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1. Glu-Glu Dipeptidase

Author

J. Ken McDonald

Subjects
Dipeptidase, chemistry.chemical_classification, biology, education, Proteolytic enzymes, humanities, Structural chemistry, body regions, surgical procedures, operative, Enzyme, chemistry, Biochemistry, Cleave, biology.protein, health care economics and organizations
Abstract

The third edition of the Handbook of Proteolytic Enzymes aims to be a comprehensive reference work for the enzymes that cleave proteins and peptides, and contains over 800 chapters. Each chapter is organized into sections describing the name and history, activity and specificity, structural chemistry, preparation, biological aspects, and distinguishing features for a specific peptidase. The subject of Chapter 829 is Glu-Glu Dipeptidase.

Published
2013
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4. Contributors

Author

Catherine Anne Abbott, Carmela R. Abraham, Hideki Adachi, Osao Adachi, Zach Adam, Michael W.W. Adams, Michael J. Adang, Ibrahim M. Adham, Patrizia Aducci, David A. Agard, Alexey A. Agranovsky, Tetsuya Akamatsu, Yoshinori Akiyama, Reidar Albrechtsen, Alí Alejo, Sean M. Amberg, Alexander Y. Amerik, Piti Amparyup, Felipe Andrade, Germán Andrés, Daniel M. Andrews, Robert K. Andrews, Toni M. Antalis, Colin S. Anthony, Naoya Aoki, Suneel S. Apte, Kazunari Arima, Gérard Arlaud, Raghuvir Krishnaswamy Arni, Pascal Arnoux, Nathan N. Aronson, Michel Arthur, Yasuhisa Asano, Paolo Ascenzi, Marina T. Assakura, David S. Auld, Veridiana de Melo Rodrigues Ávila, Francesc X. Avilés, William M. Awad, Anand K. Bachhawat, Shan Bai, Teaster T. Baird, S. Paul Bajaj, Susan C. Baker, Agnieszka Banbula, Alan J. Barrett, Jemima Barrowman, John D. Bartlett, Jörg W. Bartsch, Nikola Baschuk, Isolda P. Baskova, Jyotsna Batra, Karl Bauer, Ulrich Baumann, Wolfgang Baumeister, Cédric Bauvois, Alex Bayés, Anne Beauvais, Christoph Becker-Pauly, Tadhg P. Begley, Miklós Békés, Robert Belas, Daniah Beleford, Teruhiko Beppu, Ernst M. Bergmann, Bruno A. Bernard, Dominique Bernard, Michael C. Berndt, Giovanna Berruti, Colin Berry, Greg P. Bertenshaw, Christian Betzel, Chetana Bhaskarla, Manoj Bhosale, Gabriele Bierbaum, B. Bjarnason Jón, Michael Blaber, Michael J. Blackman, Alexander Blinkovsky, Jef D. Boeke, Matthew Bogyo, Stefan Bohn, Guy Boileau, Mike Boland, Tové C. Bolken, Judith S. Bond, Jan Bondeson, Javier Bordallo, Claudia Borelli, Tiago O. Botelho, Richard R. Bott, David G. Bourne, Niels Bovenschen, Ralph A. Bradshaw, Klaus Breddam, Keith Brew, Paul J. Brindley, Diane L. Brinkman, Collette Britton, Jeff R. Broadbent, Anne Broadhurst, Dieter Brómme, Murray Broom, Jeremy S. Brown, Mark A. Brown, Iris Bruchhaus, Barbara A. Burleigh, Kristin E. Burns, James F. Burrows, Michael J. Butler, David J. Buttle, Chelsea M. Byrd, Tony Byun, Sandrine Cadel, Conor R. Caffrey, Santiago Cal, Javier Caldentey, Thomas Candela, Clemente Capasso, Daniel R. Capriogilio, Vincenzo Carginale, Adriana Karaoglanovic Carmona, Vern B. Carruthers, Francis J. Castellino, Joseph J. Catanese, Bruce Caterson, George H. Caughey, Naimh X. Cawley, Tim E. Cawston, Juan José Cazzulo, Jijie Chai, Karl X. Chai, Olga Meiri Chaim, L.S. Chang, Julie Chao, Marie-Pierre Chapot-Chartier, Jean-Louis Charli, Paulette Charlier, Karen J. Chave, Jian-Min Chen, Jinq-May Chen, Li-Mei Chen, Ya-Wen Chen, Yu-Yen Chen, Bernard Chevrier, Jean-François Chich, Jeremy Chien, Suneeta Chimalapati, Ki Joon Cho, Kwan Yong Choi, Woei-Jer Chuang, Chin Ha Chung, Ivy Yeuk Wah Chung, Christine Clamagirand, Ian M. Clark, Adrian K. Clarke, Nicola E. Clarke, Steven Gerard Clarke, Philippe Clauziat, Judith A. Clements, Catherine Coffinier, Paul Cohen, Alain Colige, Anne Collignon, Sean D. Colloms, Andreas Conzelmann, Graham H. Coombs, Jakki C. Cooney, Jonathan B. Cooper, Max D. Cooper, Nikki A. Copeland, Graeme S. Cottrell, Joseph T. Coyle, Charles S. Craik, John W.M. Creemers, Daniela Cretu, Jenifer Croce, Keith J. Cross, Rosario Cueva, Sheng Cui, Luis Cunha, Simon Cutting, Christophe d’Enfert, Hugues D’Orchymont, Björn Dahlbäck, Shujia Dai, Ross E. Dalbey, John P. Dalton, Pam M. Dando, R.M. Daniel, Sergei M. Danilov, Donna E. Davies, Heloisa S. De Araujo, Teresa De los Santos, Viviana de Luca, Ingrid De Meester, Ana Karina de Oliveira, Eduardo Brandt de Oliveira, Pedro Lagerblad De Oliveira, Sarah de Vos, Jeroen Declercq, Wim Declercq, Ala-Eddine Deghmane, Niek Dekker, Sonia Del Prete, Marina Del Rosal, Bernard Delmas, Robert DeLotto, Ilya V. Demidyuk, Mark R. Denison, Jan M. Deussing, Lakshmi A. Devi, Eleftherios P. Diamandis, Isabel Diaz, Araceli Díaz-Perales, Bauke W. Dijkstra, Yan Ding, Jack E. Dixon, Johannes Dodt, Terje Dokland, Iztok Dolenc, Ningzheng Dong, Tran Cat Dong, Ying Dong, Mitesh Dongre, Mark Donovan, Timothy M. Dore, Loretta Dorstyn, Hong Dou, Zhicheng Dou, Annette M. Dougall, Marcin Drag, Edward G. Dudley, Ben M. Dunn, Bruno Dupuy, Maria Conceicāo Duque-Magalhāes, M. Asunción Durá, Yves Eeckhout, Vincent Eijsink, Arthur Z. Eisen, Azza Eissa, Sandra Eklund, Ziad M. Eletr, Vincent Ellis, Wolfgang Engel, Ervin G. Erdös, Teresa Escalante, David A. Estell, Michael Etscheid, Herbert J. Evans, Roger D. Everett, Alex C. Faesen, Falk Fahrenholz, Miriam Fanjul-Fernández, Christopher J. Farady, Georges Feller, Hong Feng, Kurt M. Fenster, Claude Férec, Silvia Ferrari, Barbara Fingleton, Jed F. Fisher, Paula M. Fives-Taylor, Loren G. Fong, F. Forneris, Brian M. Forster, Friedrich Forster, Simon J. Foster, Thierry Foulon, Stephen I. Foundling, Jay William Fox, Bruno Franzetti, Alejandra P. Frasch, Hudson H. Freeze, Jean-Marie Frère, Teryl K. Frey, Beate Fricke, Lloyd D. Fricker, Rafael Fridman, Christopher J. Froelich, Camilla Fröhlich, Hsueh-Liang Fu, Cynthia N. Fuhrmann, Satoshi Fujimura, Hiroshi Fujiwara, Jun Fukushima, Keiichi Fukuyama, Robert S. Fuller, Martin Fusek, Christine Gaboriaud, Christian Gache, Oleksandr Gakh, Peter Gal, Junjun Gao, Adolfo García-Sastre, Donald L. Gardiner, John A. Gatehouse, G.M. Gaucher, Francis Gauthier, Jean-Marie Ghuysen, Wade Gibson, Jennifer Gillies, Elzbieta Glaser, Fabian Glaser, Michael H. Glickman, Peter Goettig, Colette Goffin, Eiichi Gohda, Alfred L. Goldberg, Daniel E. Goldberg, Gregory I. Goldberg, Nathan E. Goldfarb, F. Xavier Gomis-Rüth, B. Gopal, Alexander E. Gorbalenya, Stuart G. Gordon, Mark D. Gorrell, Friedrich Götz, Theodoros Goulas, Cécile Gouzy-Darmon, K. Govind, Lászlo Gráf, Robert R. Granados, Melissa Ann Gräwert, Douglas A. Gray, Thomas P. Graycar, Jonathan A. Green, Luiza Helena Gremski, Michael Groll, Tania Yu Gromova, P. Gros, Marvin J. Grubman, Amy M. Grunden, Ágústa Gudmundsdóttir, Micheline Guinand, Djamel Gully, Alla Gustchina, José María Gutiérrez, Byung Hak Ha, Jesper Z. Haeggström, James H. Hageman, Johanna Haiko, Stephan Hailfinger, Hans Michael Haitchi, Ji Seon Han, Chantal Hanquez, Minoru Harada, Ikuko Hara-Nishimura, Marianne Harboe, Torleif Härd, David A. Harris, Ulrich Hassiepen, Shoji Hata, Akira Hattori, Rong-Qiao He, Albert J.R. Heck, Dirk F. Hendricks, Bernhard Henrich, Patrick Henriet, Andrés Hernández-Arana, Irma Herrera-Camacho, Gerhard Heussipp, Toshihiko Hibino, P.M. Hicks, Bradley I. Hillman, B. Yukihiro Hiraoka, Jun Hiratake, Yohei Hizukuri, Heng-Chien Ho, Ngo Thi Hoa, Mark Hochstrasser, Kathryn M. Hodge, Theo Hofmann, Thomas Hohn, John R. Hoidal, Joachim-Volker Höltje, Koichi J. Homma, John F. Honek, Vivian Y.H. Hook, John D. Hooper, Nigel M. Hooper, Kazuo Hosoi, Christopher J. Howe, Dennis E. Hruby, James J.-D. Hseih, Chun-Chieh Hsu, Tony T. Huang, Tur-Fu Huang, Yoann Huet, Clare Hughes, Jean-Emmanuel Hugonnet, Adrienne L. Huston, Oumaïma Ibrahim-Granet, Eiji Ichishima, Yukio Ikehara, Tadashi Inagami, Jessica Ingram, R.E. Isaac, Grazia Isaya, Clara E. Isaza, Shin-ichi Ishii, Amandine Isnard, Kiyoshi Ito, Koreaki Ito, Yoshifumi Itoh, Xavier Iturrioz, Sadaaki Iwanaga, Ralph W. Jack, Mel C. Jackson, Michael N.G. James, Jiří Janata, Claire Janoir, Hanna Janska, Ken F. Jarrell, Mariusz Jaskolski, Sheila S. Jaswal, Ying Y. Jean, Dieter E. Jenne, Young Joo Jeon, Ping Jiang, John E. Johnson, Michael D. Johnson, James A. Johnston, Amanda Jones, Elizabeth W. Jones, Carine Joudiou, Luiz Juliano, Hea-Jin Jung, Ray Jupp, Todd F. Kagawa, Hubert Kalbacher, Yayoi Kamata, Shuichi Kaminogawa, Yoshiyuki Kamio, Makoto Kaneda, Sung Gyun Kang, Sung Hwan Kang, Mary Kania, Tomasz Kantyka, Nobuyuki Kanzawa, Abdulkarim Y. Karim, Takafumi Kasumi, Hiroaki Kataoka, Hardeep Kaur, Shun-Ichiro Kawabata, Mari Kawaguchi, John Kay, Murat Kaynar, Kenneth C. Keiler, R.M. Kelly, Nathaniel T. Kenton, Michael A. Kerr, Kristof Kersse, Jukka Kervinen, Benedikt M. Kessler, Efrat Kessler, Timo K. Khoronen, Simon Kidd, Marjolein Kikkert, Mogens Kilian, Do-Hyung Kim, Doyoun Kim, Eunice EunKyeong Kim, In Seop Kim, Jung-Gun Kim, Kyeong Kyu Kim, Kyung Hyun Kim, Matthew S. Kimber, Yukio Kimura, Heidrun Kirschke, Yoshiaki Kiso, Colin Kleanthous, Jürgen R. Klein, Michael Klemba, Beata Kmiec, Hideyuki Kobayashi, Hiroyuki Kodama, Gerald Koelsch, Jan Kok, P.E. Kolattukody, Fabrice A. Kolb, Harald Kolmar, Yumiko Komori, Jan Konvalinka, Brice Korkmaz, Sergey V. Kostrov, Hans-Georg Kräusslich, Gabi Krczal, Lawrence F. Kress, Magnüs Már Kristjánsson, Tomáš Kučera, Sayali S. Kukday, Hidehiko Kumagai, Sharad Kumar, Malika Kumarasiri, Takashi Kumazaki, Beate M. Kümmerer, Kouji Kuno, Markku Kurkinen, Eva Kutejová, Marie Kveiborg, Agnieszka Kwarciak, Liisa Laakkonen, Nikolaos E. Labrou, Gavin D. Laing, Gayle Lamppa, Thomas Langer, Richard A. Laursen, Richard A. Lawrenson, Matthew D. Layne, Bernard F. Le Bonniec, María C. Leal, Ronald M. Lechan, David H. Lee, Irene Lee, Jae Lee, Kye Joon Lee, Soohee Lee, Xiaobo Lei, Jonathan Leis, Ellen K. LeMosy, Thierry Lepage, Stephen H. Leppla, Adam Lesner, Ivan A.D. Lessard, Guy Lhomond, Huilin Li, Shu-Ming Li, Weiguo Li, Ta-Hsiu Liao, Robert C. Liddington, Toby Lieber, H.R. Lijnen, Christopher D. Lima, Chen-Yong Lin, Gang Lin, Ming T. Lin, Xinli Lin, Yee-Shin Lin, L.L. Lindsay, William N. Lipscomb, John W. Little, Ching-Chuan Liu, Chuan-ju Liu, Mark O. Lively, Nurit Livnat-Levanon, Per O. Ljungdahl, Catherine Llorens-Cortes, Peter Lobel, Y. Peng Loh, Jouko Lohi, G.P. Lomonossoff, Yvan Looze, Carlos López-Otin, Landys Lopez-Quezada, Alex Loukas, Long-Sheng Lu, Áke Lundwall, Liu-Ying Luo, Andrei Lupas, Dawn S. Luthe, Nicholas J. Lynch, Peter J. Lyons, Vivian L. MacKay, Jesica M. Levingston Macleod, Viktor Magdolen, Jean-Luc Mainardi, Kauko K. Mäkinen, Jeremy P. Mallari, Surya P. Manandhar, Fajga R. Mandelbaum, Anne M. Manicone, Johanna Mansfeld, Joseph Marcotrigiano, Michael Mares, Gemma Marfany, Francis S. Markland, Judith Marokházi, Hélène Marquis, Robert A. Marr, Enzo Martegani, Erik W. Martin, Manuel Martinez, L. Miguel Martins, Masato Maruyama, Masugi Maruyama, Sususmu Maruyama, Takeharu Masaki, Ramin Massoumi, Rency T. Mathew, Lynn M. Matrisian, Yoshihiro Matsuda, Osamu Matsushita, Marco Matuschek, Anna Matušková, Krisztina Matúz, Cornelia Mauch, Michael R. Maurizi, Lorenz M. Mayr, Dewey G. McCafferty, J. Ken McDonald, James H. McKerrow, David McMillan, Robert P. Mecham, Darshini P. Mehta, Chris Meisinger, Alan Mellors, Roger G. Melton, Jeffrey A. Melvin, Robert Ménard, Luis Menéndez-Arias, Milene C. Menezes, Andrew Mesecar, Stéphane Mesnage, Diane H. Meyer, Gregor Meyers, Susan Michaelis, Karolina Michalska, Wojciech P. Mielicki, Igor Mierau, Galina V. Mikoulinskaia, Charles G. Miller, Lydia K. Miller, John Mills, Kenneth V. Mills, Jinrong Min, Michel-Yves Mistou, Yoshio Misumi, Shin-ichi Miyoshi, Shigehiko Mizutani, Shahriar Mobashery, Satsuki Mochizuki, William L. Mock, Frank Möhrlen, Nathalie Moiré, Paul E. Monahan, Angela Moncada-Pazos, Véronique Monnet, Michel Monod, Cesare Montecucco, Laura Morelli, Sumiko Mori, Takashi Morita, James H. Morrissey, Richard J. Morse, John S. Mort, Uffe H. Mortensen, Rory E. Morty, Joel Moss, Hidemasa Motoshima, Jeremy C. Mottram, Ana M. Moura-da-Silva, Mary Beth Mudgett, Egbert Mundt, Kazuo Murakami, Mario Tyago Murakami, Kimiko MurakamiMurofoshi, Sawao Murao, Gillian Murphy, M.R.N. Murthy, Tatsushi Muta, Elmarie Myburgh, Nino Mzhavia, A.H.M. Nurun Nabi, Hideaki Nagase, Michael W. Nagle, Dorit K. Nägler, Rajesh R. Naik, Divya B. Nair, Toshiki Nakai, Yoshitaka Nakajima, Yukio Nakamura, Hitoshi Nakatogawa, Toru Nakayama, Natalia N. Nalivaeva, Dipankar Nandi, Maria Clara Leal Nascimento-Silva, Kim Nasmyth, Carl F. Nathan, Fernando Navarro-García, Dayane Lorena Naves, Danny D. Nedialkova, Keir C. Neuman, Jeffrey-Tri Nguyen, Ky-Anh Nguyen, Gabriela T. Niemirowicz, Toshiaki Nikai, Eiichiro Nishi, Wataru Nishii, Makoto Nishiyama, Yasuhiro Nishiyama, Masatoshi Noda, Seiji Nomura, Shigemi Norioka, Desire M.M. Nsangou, Amornrat O’Brien, Michael B. O’Connor, Kohei Oda, Irina V. Odinokova, Joyce Oetjen, Teru Ogura, Dennis E Ohman, Yoshinori Ohsumi, Mukti Ojha, Akinobu Okabe, Yasunori Okada, Keinosuke Okamoto, Kenji Okuda, Nobuaki Okumura, Takashi Okuno, Kjeld Oleson, Priscila Oliveira de Giuseppe, Martin Olivier, Yasuko Ono, Stephen Oroszlan, Nobuyuki Ota, Michael Ovadia, Jiyang O-Wang, Claus Oxvig, Jeremy C.L. Packer, Sergio Padilla-López, Mark Paetzel, Michael J. Page, Andrea Page-McCaw, Mark J.I. Paine, Byoung Chul Park, Eunyong Park, John E. Park, Pyong Woo Park, Sung Goo Park, Kirk L. Parkin, William C Parks, Thaysa Paschoalin, Annalisa Pastore, Alexander Nikolich Patananan, Sudhir Paul, Henry L. Paulson, Ulrich von Pawel-Rammingen, David A. Pearce, Mark S. Pearson, Duanqing Pei, Gunnar Pejler, Alan D. Pemberton, Jianhao Peng, Julien Pernier, Jan-Michael Peters, Thorsten Pfirrmann, Viet-Laï Pham, Iva Pichová, Darren Pickering, Christophe Piesse, David Pignol, Robert N. Pike, Lothaire Pinck, Hubert Pirkle, Henry C. Pitot, Andrew G. Plaut, Hidde Ploegh, László Polgár, Corrine Porter, Rolf Postina, Jan Potempa, Knud Poulsen, Scott D. Power, Rex. F. Pratt, Gerd Prehna, Gilles Prévost, Alexey V. Pshezhetsky, Mohammad A. Qasim, Feng Qian, Jiazhou Qiu, Víctor Quesada, Evette S. Radisky, Stephen D. Rader, Kavita Raman, Andrew J. Ramsay, Derrick E. Rancourt, Najju Ranjit, Narayanam V. Rao, Kiira Ratia, Neil D. Rawlings, Robert B. Rawson, Vijay Reddy, Colvin M. Redman, Maria Elena Regonesi, Andreas S. Reichert, Antonia P. Reichl, Han Remaut, S. James Remington, Martin Renatus, David Reverter, Eric C. Reynolds, Mohamed Rholam, Charles M. Rice, Todd W. Ridky, Howard Riezman, D.C. Rijken, Marie-Christine Rio, Alison Ritchie, Janine Robert-Baudouy, Mark W. Robinson, Michael Robinson, Adela Rodriguez-Romero, Renata Santos Rodriques, John C. Rogers, Camilo Rojas, Floyd E. Romesberg, David J. Roper, Nora Rosas-Murrieta, A.M. Rose, Philip J. Rosenthal, J. Rosing, Ornella Rossetto, Véronique Rossi, Richard A. Roth, Hanspeter Rottensteiner, Andrew D. Rowan, Mikhail Rozanov, Alexandra Rucavado, Andrea Ruecker, Françoise Rul, Till Rümenapf, Ilaria Russo, Martin D. Ryan, Elena Sacco, J. Evan Sadler, W. Saenger, Hans-Georg Sahl, Mohammed Sajid, Masayoshi Sakaguchi, Fumio Sakiyama, Maria L. Salas, Maria Cristina O. Salgado, Guy S. Salvesen, Edith Sánchez, Eladio F. Sanchez, Qing-Xiang Amy Sang, Krishnan Sankaran, Susanta K. Sarkar, Michael P. Sarras, Yoshikiyo Sasagawa, Araki Satohiko, Eric Sauvage, Loredana Saveanu, H.S. Savithri, Hitoshi Sawada, R. Gary Sawers, Isobel A. Scarisbrick, Andreas Schaller, Justin M. Scheer, Friedrich Scheiflinger, Cordelia Schiene-Fischer, Uwe Schlomann, Manfred Schlösser, Alvin H. Schmaier, Walter K. Schmidt, Anette Schneemann, Rick G. Schnellmann, Henning Scholze, Lutz Schomburg, Wilhelm J. Schwaeble, Christopher J. Scott, Rosaria Scudiero, Atsuko Sehara-Fujisawa, Nabil G. Seidah, Motoharu Seiki, Junichi Sekiguchi, Andrea Senff-Ribeiro, Ihn Sik Seong, Mihaela Serpe, Solange M.T. Serrano, Peter Setlow, Tina Shahian, M. Shanks, Feng Shao, Steven D. Shapiro, Navneet Sharma, Lindsey N. Shaw, Aimee Shen, Lei Shen, Roger F. Sherwood, Yun-Bo Shi, Hitoshi Shimoi, Yoichiro Shimura, A.D. Shirras, Viji Shridhar, Jinal K. Shukla, Ene Siigur, Jüri Siigur, Natalie C. Silmon de Monerri, Robert B. Sim, James P. Simmer, William H. Simmons, Jaspreet Singh, Alison Singleton, Tatiana D. Sirakova, Titia K. Sixma, Tim Skern, Randal A. Skidgel, Jeffrey Slack, David E. Sleat, Barbara S. Slusher, Janet L. Smith, Matthew A. Smith, Mark J. Smyth, Erik J. Snijder, Solmaz Sobhanifar, Kenneth Söderhaäll, Istvan Sohar, Peter Sonderegger, Marcos Henrique Ferreira Sorgine, Hiroyuki Sorimachi, Karen E. Soukhodolets, Tatiana de Arruda Campos Brasil de Souza, Tamás Sperka, Shiranee Sriskandan, Joseph W. St. Geme, Raymond J. St. Leger, Peter Staib, James L. Steele, Bjarki Stefansson, Christian Steinkühler, Leisa M. Stenberg, Johan Stenflo, Henning R. Stennicke, Valentin M. Stepanov, Olga A. Stepnaya, Frank Steven, Richard L. Stevens, Kenneth J. Stevenson, Mathieu St-Louis, Christopher C. Stobart, Walter Stöcker, Andrew C. Storer, Norbert Sträter, Ellen G. Strauss, James H. Strauss, Kvido Stříšovský, Natalie C.J. Strynadka, Edward D. Sturrock, Dan Su, Xiao-Dong Su, Paz Suárez-Rendueles, Traian Sulea, Venkatesh Sundararajan, Ryoji Suno, Carolyn K. Suzuki, Fumiaki Suzuki, Hideyuki Suzuki, Nobuhiro Suzuki, Stephen Swenson, Rose L. Szabady, Pal Bela Szecsi, Lászlo Szilágyi, Muhamed-Kheir Taha, Eizo Takahashi, Kenji Takahashi, Toshiro Takai, Atsushi Takeda, Soichi Takeda, Jeremy J.R.H. Tame, Tomohiro Tamura, Fulong Tan, Keiji Tanaka, Carmen Tanase, Jordan Tang, Martha M. Tanizaki, Egbert Tannich, Guido Tans, Anthony L. Tarentino, Anchalee Tassanakajon, Hiroki Tatsumi, Norbert Tautz, Erin Bassford Taylor, Pedro Filipe Teixeira, Bhanu Prakash V.L. Telugu, Markus F. Templin, Shigeyuki Terada, Uchikoba Tetsuya, C. Thacker, Maulik Thaker, Heinz-Jürgen Thiel, Nicole Thielens, Gonzales Thierry, Karine Thivierge, Mark D. Thomas, Margot Thome, Mary K. Thorsness, Peter E. Thorsness, Natalie J. Tigue, Sokol V. Todi, Birgitta Tomkinson, Fiorella Tonello, Liang Tong, H.S. Toogood, Paolo Tortora, József Tözsèr, Luiz Rodolpho Travassos, James Travis, Dilza Trevisan-Silva, Francesca Trinchella, Neil N. Trivedi, Carol M. Troy, Harald Tschesche, Yu-Lun Tseng, Masafumi Tsujimoto, Anthony T. Tu, Kathleen E. Tumelty, Boris Turk, Dusan Turk, Vito Turk, Anthony J. Turner, Tetsuya Uchikoba, Takayuki Ueno, Alejandro P. Ugalde, Veli-Jukka Uitto, Sinisa Urban, Olivier Valdenaire, Adrian Valli, Jozef Van Beeumen, Bertus Van den Burg, Renier A.L. Van der Hoorn, Jan Maarten van Dijl, Peter Van Endert, Bram J. Van Raam, Harold E. Van Wart, Tom Vanden Berghe, Peter Vandenabeele, Margo Vanoni, Silvio Sanches Veiga, William H. Velander, Gloria Velasco, Josep Vendrell, I. István Venekei, Vaclav Vetvicka, F.-Nora Vögtle, Waldemar Vollmer, Kei Wada, Fred W. Wagner, Sun Nyunt Wai, Timothy Wai, Shane Wainwright, Kenneth W. Walker, Stephen J. Walker, Jean Wallach, Linda L. Walling, Peter N. Walsh, Hai-Yan Wang, Hengbin Wang, Jianwei Wang, Peng Wang, Ping Wang, Michael Wassenegger, Kunihiko Watanabe, Helen Webb, Joseph M. Weber, Niklas Weber, Daniel R. Webster, Shuo Wei, Rodney A. Welch, James A. Wells, Herbert Wenzel, Ingrid E. Wertz, Ulla W. Wewer, Alison R. Whyteside, Sherwin Wilk, Jean-Marc Wilkin, Claudia Wilmes, Jakob R. Winther, David S. Wishart, Alexander Wlodawer, J. Fred Woessner, Michael S. Wolfe, Wilson Wong, Roger Woodgate, Gerry Wright, Jiunn-Jong Wu, Qingyu Wu, Magdalena Wysocka, Chao Xu, Zhenghong Xu, Kinnosuke Yahori, Shoji Yamada, Nozomi Yamaguchi, Shinji Yamaguchi, Yoshio Yamakawa, Hiroki Yamamoto, Ikao Yana, Maozhou Yang, Na Yang, Chenjuan Yao, Tingting Yao, Noriko Yasuda, Toshimasa Yasuhara, Shigeki Yasumasu, Edward T.H. Yeh, Irene Yiallouros, Jiang Yin, Hiroo Yonezawa, Soon Ji Yoo, Tadashi Yoshimoto, Michael W. Young, Stephen G. Young, Nousheen Zaidi, Ludmila L. Zavalova, Peter Zavodszky, Aidong Zhang, Xianming Zhang, Yi-Zheng Zhang, Dominick Zheng, Guangming Zhong, Rong Zhong, Yuan Zhou, Zhaohui Sunny Zhou, Michael Zick, Paola Zigrino, and Andrei A. Zimin

Published
2013
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8. Dipeptidyl peptidase III of human cataractous lenses. Partial purification

Author

J. Ken McDonald, Arnold A. Swanson, and Rebecca M. Davis

Subjects
Proteases, Hot Temperature, Biology, Cataract, Cellular and Molecular Neuroscience, chemistry.chemical_compound, Endopeptidases, Lens, Crystalline, Chemical Precipitation, Humans, Dipeptidyl-Peptidases and Tripeptidyl-Peptidases, Leucyl aminopeptidase, Neprilysin, Aqueous extract, Chromatography, Hydrolysis, Substrate (chemistry), Dipeptides, Crystallins, Sensory Systems, Ophthalmology, chemistry, Biochemistry, Puromycin, Specific activity, Dipeptidyl-peptidase III
Abstract

A partial purification of dipeptidyl peptidase III has been achieved from human cataractous lens. The specific activity was increased 45.5-fold over that of the original aqueous extract. The exopeptidase exhibited a marked preference for the release of Arg-Arg from Arg-Arg-2-NNap at the optimum pH 8.8 and 37 degrees. The Km for this substrate was estimated to be 6.061 X 10(-3). Lens DPP III was inhibited by EDTA, p-chloromercuriphenyl sulfonate, puromycin and DFP. The preparation contained leucyl aminopeptidase and a neutral endopeptidase as contaminating proteases.

Published
1984
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9. Mammalian lens dipeptidyl aminopeptidase III

Author

J. Ken McDonald, Arnold A. Swanson, and Barbara Albers-Jackson

Subjects
Arginine, Biophysics, Biochemistry, Aminopeptidase, Substrate Specificity, chemistry.chemical_compound, Drug Stability, Endopeptidases, Lens, Crystalline, Animals, Molecular Biology, Alanine, chemistry.chemical_classification, biology, Dipeptides, Cell Biology, Exopeptidase, Molecular biology, Kinetics, Enzyme, chemistry, Puromycin, biology.protein, Cattle, Alanine aminopeptidase, Leucine
Abstract

An intracellular exopeptidase identified as dipeptidyl aminopeptidase III (DAP III) was found to be abundant in the bovine lens. The enzyme contained in aqueous extracts exhibited a marked preference, compared to other dipeptidyl-β-naphthylamides, for the release of Arg-Arg from Arg-Arg-2-NNap at the optimum pH 9.0 and 37°. The K m for this substrate was estimated to be 2.83 × 10 −5 M. Lens DAP III was inhibited by EDTA, p-chloromercuriphenyl sulfonate, and puromycin. Lens aminopeptidase activities measured at pH 7.5 on the β-naphthylamides of leucine, alanine, and arginine, included for comparison, suggested that not only is leucine aminopeptidase abundant, but also other aminopeptidases that appear to include alanine aminopeptidase and aminopeptidase B.

Published
1978
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11. Inactivation and Degradation of Glucagon by Dipeptidyl Aminopeptidase I (Cathepsin C) of Rat Liver

Author

Benjamin B. Zeitman, J. Ken McDonald, Paul X. Callahan, and Stanley Ellis

Subjects
Cathepsin, endocrine system, endocrine system diseases, Arginine, biology, Chemistry, digestive, oral, and skin physiology, Cell Biology, digestive system, Biochemistry, Glucagon, Enzyme assay, Secretin, Cathepsin C, Paper chromatography, biology.protein, Secretion, Molecular Biology
Abstract

Chloride and sulfhydryl activators in glucagol degradation and secretion by purified rat liver dipeptidyl aminopeptidase I /Cathepsin C/

Published
1969
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12. The hydrolysis of amino acyl-β-naphthylamides by plasma aminopeptidases

Author

Stanley Ellis, J. Ken McDonald, and Thomas J. Reilly

Subjects
Human blood, Carbon Tetrachloride Poisoning, Biophysics, Cobalt, Haplorhini, Neoplasms, Experimental, Cell Biology, Naphthalenes, Biology, Aminopeptidases, Biochemistry, Aminopeptidase, Rats, Kinetics, Leucyl Aminopeptidase, Hydrolysis, Blood plasma, Tissue extracts, Animals, Humans, Puromycin, Sulfhydryl Compounds, Leucine, Molecular Biology
Abstract

Historically, the study of aminopeptidase activity in mammalian systems has been directed primarily toward tissue extracts. This work culminated in the isolation and characterization of the classical leucine aminopeptidase ( Smith and Hill, 1960 ). Little attempt has been made to characterize the aminopeptidases of normal plasma and serum, and perhaps it is for this reason that the activity has been tacitly identified with tissue leucine aminopeptidase (LAP), and commonly designated serum LAP. Behal et al. (1963) have chromatographically resolved the LAP activity of human blood into a number of aminopeptidase components. In this report, some distinguishing properties are described for a variety of aminopeptidases which can occur in blood plasma. The aminopeptidase activity of normal plasma could not be attributed to the presence of leucine aminopeptidase.

Published
1964
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13. Properties of Dipeptidyl Arylamidase I of the Pituitary

Author

J. Ken McDonald, Thomas J. Reilly, and Stanley Ellis

Subjects
chemistry.chemical_classification, endocrine system, endocrine system diseases, biology, Chemistry, Stereochemistry, digestive, oral, and skin physiology, Peptide, Cell Biology, digestive system, Biochemistry, Chloride, Enzyme assay, Catalysis, chemistry.chemical_compound, Hydrolysis, Amide, medicine, biology.protein, Beta-naphthylamide, Molecular Biology, medicine.drug
Abstract

Dipeptidyl arylamidase I of bovine pituitary tissue and chloride and sulfhydryl activation of seryltyrosyl-beta-naphthylamide hydrolysis

Published
1966
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14. Angiotensinase Activity of Dipeptidyl Aminopeptidase I (Cathepsin C) of Rat Liver

Author

Stanley Ellis, Benjamin B. Zeitman, J. Ken McDonald, and Paul X. Callahan

Subjects
chemistry.chemical_classification, Dipeptide, biology, Biological activity, Cell Biology, Biochemistry, Angiotensin II, Enzyme assay, Cathepsin C, Amino acid, Turnover number, chemistry.chemical_compound, Enzyme, chemistry, biology.protein, Molecular Biology
Abstract

Dipeptidyl aminopeptidase I (cathepsin C) purified from rat liver was shown to have marked angiotensinase activity arising from its ability to catalyze the rapid removal of two dipeptide fragments, in succession, from the NH2 terminus of a variety of angiotensin II analogues. The most rapid rates of degradation were observed on Asn1-angiotensin II (Hypertensin, Ciba), angiotensin II (bovine), and Ile5-angiotensin II (human). Kinetic studies with the first (Km = 0.44 mm) and the last (Km = 0.34 mm) showed essentially the same turnover number (5220 min-1) for the removal of the first dipeptide at pH 5.0 and 37°. The Km for α-Asp-Arg-β-naphthylamide (a model, fluorogenic substrate) was 0.31 mm. Unnatural, biologically active analogues such as β-Asp1-angiotensin II and α-d-Asp1-angiotensin II were also degraded, although at lower rates. No action was detected on Asn1, d-Arg2-angiotensin II. The degradation of Asn1-angiotensin II and Ile5-angiotensin II by dipeptidyl amino-peptidase I was pronounced over a wide range of pH (3 to 7.5) with a maximum between pH 5 and 6. About 20% of the (pH 7.3) activity of the purified enzyme was manifested when added to rat blood plasma that did not contain added Cl- and —SH activators. The predominant products and course of angiotensin II degradation at pH 5.5 by isolated rat liver lysosomes were identical with those produced by purified dipeptidyl aminopeptidase I, thereby demonstrating that this enzyme is probably the major contributor to the angiotensinase activity of liver lysosomes.

Published
1974
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15. A chloride-activated dipeptidyl-β-naphthylamidase of the pituitary gland

Author

Stanley Ellis, J. Ken McDonald, and Thomas J. Reilly

Subjects
endocrine system, Pituitary gland, medicine.medical_specialty, endocrine system diseases, In Vitro Techniques, Naphthalenes, digestive system, Chloride, Fluorescence, General Biochemistry, Genetics and Molecular Biology, Amidohydrolases, Amidase, Chlorides, stomatognathic system, Anterior pituitary, Internal medicine, medicine, Animals, General Pharmacology, Toxicology and Pharmaceutics, chemistry.chemical_classification, digestive, oral, and skin physiology, Dipeptides, General Medicine, medicine.anatomical_structure, Enzyme, Endocrinology, chemistry, Biochemistry, Pituitary Gland, Cattle, Colorimetry, Puromycin, medicine.drug
Abstract

Dipeptidyl-beta-naphthylamidase activated by chloride in extracts of rat and bovine anterior pituitary glands

Published
1965
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16. Oxidase activity and lipid composition of respiratory particles from Claviceps purpurea (Ergot fungus)

Author

F.Kang Sun, Vernon H. Cheldelin, J. Ken McDonald, and Jay Anderson

Subjects
Citric Acid Cycle, Biophysics, Antimycin A, Biology, Biochemistry, Claviceps, Electron Transport Complex IV, chemistry.chemical_compound, Ascomycota, Cytochrome c oxidase, Molecular Biology, Phospholipids, Phosphatidylethanolamine, Oxidase test, Cyanides, Research, Cytochrome c, Succinate dehydrogenase, Proteins, Phosphorus, Succinates, Metabolism, Claviceps purpurea, biology.organism_classification, Lipids, Mitochondria, Succinate Dehydrogenase, chemistry, biology.protein, Cytochromes, Oxidoreductases, NADP
Abstract

Respiratory particles with complete succinate and DPNH oxidase systems were prepared from vegetative cultures of Claviceps purpurea. The rates were 4–10 μmoles of succinate per hour per milligram protein at 36 °C and 20–24 μmoles of DPNH oxidized per hour per milligram at 27 °. Beef heart cytochrome c increased oxidase activity and antimycin A and cyanide completely inhibited the oxidase activity. The succinate oxidase system is rapidly disintegrated by sonic irradiation. Claviceps purpurea respiratory particles contained 26% lipid and 58% protein. There were no plasmalogens. Claviceps purpurea respiratory particles contained 10 μmoles of phosphorus per milligram lipid. The percentage of the various phospholipids was phosphatidylinositol, 28; phosphatidylcholine, 27; phosphatidylserine, 13; phosphatidylethanolamine, 18; polyglycerophosphate, 7; and residue, 7. Coenzyme Q10 (H-10) is a component of the C. purpurea respiratory particles. Claviceps purpurea respiratory lipid was slightly more effective than beef heart mitochondrial lipid in restoring the succinate-cytochrome c reductase activity of acetone-extracted beef heart mitochondria.

Published
1964
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17. Succinate dehydrogenase in the ergot fungus claviceps purpurea

Author

John A. Anderson, Vernon H. Cheldelin, J. Ken McDonald, and Tsoo E. King

Subjects
chemistry.chemical_classification, biology, Cytochrome, Chemistry, Succinate dehydrogenase, Cytochrome c, Proteolytic enzymes, Dehydrogenase, Flavin group, Biochemistry, chemistry.chemical_compound, Enzyme, Malonate, biology.protein
Abstract

1. 1. A study of electron transport by cell extracts of the parasitic fungus Claviceps purpurea revealed a succinate dehydrogenase (EC 1.3.99.1) which appeared unique among mammalian and microbial succinate dehydrogenases so far studied in respect to ease of solubilization, solubility and stability, freedom from cytochrome contamination, electron-acceptor specificity, the Km for succinate, and the nature of inhibition by iron chelators. The soluble, and relatively stable fungal succinate dehydrogenase reacted with phenazine methosulfate, whereas other electron acceptors such as triphenyltetrazolium chloride, methylene blue, 2,6-dichlorophenolindophenol, ferricyanide, and mammalian cytochrome c were ineffective. 2. 2. For the purposes of enzyme purification, it was possible directly, to extract large amounts of fungal tissue by simply blending the cells for 2 min with alumina in order to liberate succinate dehydrogenase which had never been exposed to proteolytic enzymes, organic solvents, desiccation, etc. The cell extract was clarified by ultracentrifugation, and the enzyme, located in the clear supernatant, was concentrated, partially purified, and freed of nucleic acids by conventional methods. The purified enzyme was found to be exceptionally stable, losing about 10% activity after 1 month at −15°. 3. 3. The presence of flavin in the purified preparation was ascertained by the difference spectrum for the oxidized and reduced forms of the dehydrogenase. The absorption spectra, at liquid-nitrogen temperatures, showed no contamination with cytochrome components. 4. 4. The oxidation of succinate to fumarate, catalyzed by the Claviceps dehydrogenase, showed an Arrhenius energy of activation of about 9.4 kcal at pH optimum of 7.7. The Michaelis constant for succinate, Km, was determined to be 3 mM at pH 7.7 and 35°. This was a higher value than those reported for the mammalian and yeast enzymes, but lower than the Km reported for a bacterial enzyme. 5. 5. Fumarate, pyrophosphate, and malonate were found to be competitive inhibitors of the dehydrogenation, and their respective dissociation constants, Ki, for the enzyme-inhibitor complexes, were 0.93, 0.42 and 0.03 mM. The non-competitive inhibition shown by the iron-chelating agent o-phenanthroline suggested iron to be a component of the Claviceps enzyme, but this inhibition does not necessarily reflect the essentiality or redox participation of the iron.

Published
1963
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18. On the Structure and Function of Relaxin

Author

Christian Schwabe, J. Ken McDonald, and Bernard G. Steinetz

Subjects
Relaxin, endocrine system, medicine.medical_specialty, Fetus, Insulin, medicine.medical_treatment, Biology, Structure and function, Guinea pig, Endocrinology, Internal medicine, medicine, Birth canal, hormones, hormone substitutes, and hormone antagonists, Relaxin receptor, Hormone
Abstract

The endocrinological events leading to parturition are poorly understood. There are obvious species differences and no generalizations are possible at this time. In 1926 Hisaw called attention to the fact that in some mammals an ovarian factor is produced that leads to an enlargement of the birth canal in preparation for parturition. Subsequent work showed that this factor suppressed uterine contractions that might be harmful to the fetus. Hisaw and his coworkers also demonstrated that this ovarian factor was not a steroid but a protein susceptible to proteolytic action. He determined some physical properties of his new factor, relaxin, and compared them in an almost visionary fashion with the properties of insulin. Importantly, the involvement in parturition of a distinct hormone was demonstrated for the first time. The next thirty years of relaxin research was dominated by studies concerning the physiology of relaxin. The investigation of the biochemistry of relaxin suffered from the absence of an accurate and convenient bioassay. In 1930 Fevold et al. introduced the guinea pig assay which was rather elaborate and not sufficiently objective. The introduction of the mouse assay system by Steinetz et al. (1959) and the discovery of Kliman and Greep (1958) that the activity of relaxin in mice could be enhanced more than 100-fold by simultaneous injection of an adjuvant provided a better basis for the purification of relaxin.

Published
1982
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19. Partial purification and characterization of an ovarian tripeptidyl peptidase: a lysosomal exopeptidase that sequentially releases collagen-related (Gly-Pro-X) triplets

Author

J. Ken McDonald, Donald A. Eisenhauer, and Anne R. Hoisington

Subjects
animal structures, Stereochemistry, Swine, Biophysics, Tripeptide, Biochemistry, Aminopeptidases, Tripeptidyl peptidase, Serine, Pregnancy, Animals, Molecular Biology, Fluorescent Dyes, chemistry.chemical_classification, integumentary system, biology, Chemistry, Ovary, Sulfhydryl Reagents, Cell Biology, Exopeptidase, Hydrogen-Ion Concentration, Tripeptidyl peptidase I, Amino acid, Dipeptidyl-peptidase II, Enzyme, Chromogenic Compounds, biology.protein, Electrophoresis, Polyacrylamide Gel, Female, Collagen, Lysosomes, Oligopeptides, Peptide Hydrolases, Subcellular Fractions
Abstract

The pregnant hog ovary is a rich source of a novel exopeptidase that catalyzes the release, at pH 5.0, of collagen-related (P 3 -P 2 -P 1 ) “triplets” such as Gly-Pro-Met, Gly-Pro-Arg, and Gly-Pro-Ala from arylamide derivatives, provided the N termini are unsubstituted. Corresponding derivatives of related (P 2 -P 1 ) dipeptides (Pro-Met, Pro-Ala) or (P 1 ) amino acids (Met, Arg, Ala) are not attacked. The enzyme was purified 58-fold from a detergent extract of a water-extracted tissue residue. Activity was determined on Gly-Pro-Met-2-naphthylamide at pH 4.5 and 37°C (K m 0.45 mM; V max 722 nmoles/min/mg protein). The responsible M r 55,000 exopeptidase, termed “tripeptidyl peptidase”, forms high-M r aggregates, belongs to the serine catalytic class, and has a lysosomal localization. Gly-Pro-Ala triplets were released sequentially at pH 5.0 from a M r 14,000 polypeptide, poly(Gly-Pro-Ala-). When this reaction was coupled to that of homologous dipeptidyl peptidase II, the liberated tripeptides were reduced to dipeptides and free amino acids: (Gly-Pro-Ala) n → nGly-Pro-Ala → nGly-Pro + nAla.

Published
1985

20. Dipeptidyl peptidase II of bovine dental pulp. Initial demonstration and characterization as a fibroblastic, lysosomal peptidase of the serine class active on collagen-related peptides

Author

J. Ken McDonald and Christian Schwabe

Subjects
Tripeptide, Serine, chemistry.chemical_compound, Endopeptidases, Animals, Dipeptidyl-Peptidases and Tripeptidyl-Peptidases, Dental Pulp, Serine protease, chemistry.chemical_classification, Dipeptide, biology, Chemistry, General Medicine, Fibroblasts, Hydrogen-Ion Concentration, Dipeptidyl-peptidase II, Enzyme, Biochemistry, Connective Tissue, Pituitary Gland, biology.protein, Pulp (tooth), Cattle, Female, Lysosomes, Phenylmethylsulfonyl Fluoride
Abstract

Dipeptidyl peptidase II (dipeptidylpeptide hydrolase, EC 3.4.14.2), previously known as dipeptidyl aminopeptidase II, was shown to be present in relatively high concentrations in bovine dental pulp. Based on the DNA content of tissue homogenates, the fibroblasts of this connective tissue appeared to contain more dipeptidyl peptidase II than the cells of lysosome-rich tissues such as bovine spleen and rat liver. The newly-recognized properties of dipeptidyl peptidase II, from both pulp and pituitary sources, included a marked propensity for hydrolyzing prolyl bonds at acidic pH. Lys-Pro-2-NNap and Lys-Pro-2(4-methoxy)naphthylamide (designed for cytochemical application) were hydrolyzed at rates equal to that of Lys-Ala-2-NNap. The impure pulp enzyme and the authentic pituitary enzyme showed comparable relative rates of hydrolysis on a variety of fluorogenic substrates with the general structure X-Pro-2-NNap ( X = Lys, Arg, Phe, Ala or Gly ), and on a variety of collagen-related tripeptides represented by X-Pro-Ala ( X = Gly, Ala or Lys ). The highest rates were obtained on Lys-Ala-Ala and Lys-Ala-Pro. The pH optima for the hydrolysis of the 2-naphthylamide derivatives varied from 5.0 to 5.7, and for tripeptides from 4.2 to 5.3. In all cases the N-terminal dipeptide was released intact. Although previously unrecognized as a serine protease, dipeptidyl peptidase II (of pulp and pituitary origin) was strongly inhibited by (1 mM) diisopropyl phosphorofluoridate, p- nitrophenyl -p′- guanidinobenzoate , and phenylmethylsulfonyl fluoride. The enzyme, from both sources, was fully inhibited by 0.1 mM Lys-Ala chloromethyl ketone, a newly-designed, active-site-directed inhibitor. The numerous properties shared by the putative dipeptidyl peptidase II of bovine dental pulp and an authentic preparation of the bovine pituitary enzyme provided strong support for their having a common identity.

Published
1980

21. Peptidases in Connective Tissue Degradation and Remodelling in Reproductive and Invasive Tissues

Author

Noel O. Owers, J. Ken McDonald, and Christian Schwabe

Subjects
Substrate Specificities, animal structures, biology, Chemistry, Insulin, medicine.medical_treatment, Connective tissue, Exopeptidase, Hydrolysis, medicine.anatomical_structure, Biochemistry, biology.protein, medicine, Degradation (geology), Intracellular, Macromolecule
Abstract

An outline is given of the properties and substrate specificities of three lysosomal peptidases, and of efforts to elucidate their potential role in the intracellular degradation of collagen. Use of specific fluorogenic substrates such as Gly-Phe-NNap*, Lys-Ala-NNap and Gly-Pro-Met-NMec allows direct assay of DPP I, DPP II and TPP I respectively. They may hydrolyze macromolecules as exemplified by insulin A and B chains and by poly(Gly-Pro-Ala) as a model collagen α-chain. These are extensively hydrolyzed at acidic pH by the coupled action of the three exopeptidases, which could explain the degradation of proline-rich, collagen-derived polypeptides within lysosomes lacking any known endopeptidases active at prolyl bonds.

Published
1987
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22. Relaxin

Author

CHRISTIAN SCHWABE, BERNARD STEINETZ, GERSON WEISSE, ALBERT SEGALOFF, J. KEN MCDONALD, ELIZABETH O'BYRNE, JOSEPH HOCHMAN, BYRNES CARRIERE, and LAURA GOLDSMITH

Published
1978
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23. Presence and possible role of a renal brush-border Gly-Pro-X-releasing exopeptidase

Author

Knut-Jan Andersen and J. Ken McDonald

Subjects
Male, Sucrose, Brush border, Physiology, Renal cortex, Kidney, Aminopeptidases, Dipeptidyl peptidase, Tripeptidyl peptidase, medicine, Animals, chemistry.chemical_classification, biology, Microvilli, Rats, Inbred Strains, Exopeptidase, Hydrogen-Ion Concentration, Rats, Isoenzymes, Enzyme, medicine.anatomical_structure, chemistry, Isopycnic, Biochemistry, Microsome, biology.protein, Collagen, Sodium-Potassium-Exchanging ATPase, Peptide Hydrolases, Subcellular Fractions
Abstract

Differential pelleting of a rat renal cortical homogenate clearly demonstrated the microsomal localization of an N-terminal exopeptidase of the tripeptidyl peptidase (TPP) class that typically requires a free N-terminus to catalyze the release of collagen-related (Gly-Pro-X) “triplets” at pH 7.0 (TPP 7). Once fractionated by differential pelleting, microsomal populations of different size were subfractionated by equilibrium banding in sucrose gradients for the purpose of comparing the distribution profiles and the isopycnic banding densities of TPP 7 to those for known marker enzymes. This analytical approach permitted the localization of these enzymes to specific membrane domains in the renal cortex and provided evidence for the brush-border location of TPP 7. Notably, dipeptidyl peptidase IV (DPP IV), an established plasma membrane exopeptidase with a prolyl-bond specificity, gave banding densities and distributions that were consistent with the presence of both TPP 7 and DPP IV in the same membrane compartment. Because triplets of the Gly-Pro-X type released by TPP 7 would be ideal substrates for DPP IV, a coupled TPP 7-DPP IV exopeptidase mechanism at the luminal surface (brush border) of proximal tubule cells could therefore make a major contribution to the renal degradation and reabsorption of filtered collagen fragments. tripeptidyl peptidase; aminopeptidase; collagen; rat kidney cortex Submitted on February 11, 1987 Accepted on May 13, 1987

Published
1987

24. Putative tripeptidyl peptidase in renal brush border is due to sequential action of two other exopeptidases

Author

A. John Kenny, Jean Ingram, Knut-Jan Andersen, and J. Ken McDonald

Subjects
Kidney, biology, Brush border, Microvilli, Physiology, Exopeptidase, Aminopeptidases, Tripeptidyl peptidase, medicine.anatomical_structure, Biochemistry, Endopeptidases, Exopeptidases, biology.protein, medicine, Animals, Dipeptidyl-Peptidases and Tripeptidyl-Peptidases, Peptide Hydrolases
Published
1989

25. Demonstration of a pyroglutamyl residue at the N terminus of the B-chain of porcine relaxin

Author

J. Ken McDonald and Christian Schwabe

Subjects
Relaxin, chemistry.chemical_classification, Pyrrolidonecarboxylic Acid, Swine, Biophysics, Peptide, Cell Biology, Carboxypeptidases, Peptide hormone, Biochemistry, High-performance liquid chromatography, Peptide Fragments, Pyrrolidinones, N-terminus, Residue (chemistry), chemistry, Animals, Amino Acid Sequence, Amino Acids, Molecular Biology, Hormone
Abstract

The ovarian peptide hormone relaxin consists, like insulin, of one A- and one B-chain linked by two disulfide bonds. A peptide, isolated from a tryptic digest of the purified B-chain by high-pressure liquid chromatography (HPLC), was examined with the aid of carboxypeptidase C and a pyrrolidonecarboxylyl peptidase. In conjunction with amino acid analysis it could be demonstrated that pyrrolidonecarboxylic acid occupies the N-terminal position of a peptide with the amino acid composition Asp2, Ser, Thr, Phe, Ile, Lys. The appearance of a pyroglutamyl residue in a two-chain hormone is an interesting and unusual feature which has not yet been reported in a similar structure.

Published
1977

26. Primary structure of the A chain of porcine relaxin

Author

Christian Schwabe, J. Ken McDonald, and Bernard G. Steinetz

Subjects
medicine.medical_specialty, Chromatography, Gas, Arginine, Macromolecular Substances, Swine, Phenylalanine, Biophysics, Peptide hormone, Biology, Biochemistry, Internal medicine, medicine, Animals, Insulin, Trypsin, Amino Acid Sequence, Molecular Biology, Peptide sequence, Relaxin, Protein primary structure, Tryptophan, Cell Biology, Peptide Fragments, Endocrinology, Spectrophotometry, Ultraviolet, Relaxin/insulin-like family peptide receptor 2, medicine.drug, Relaxin receptor
Abstract

The sequence of the B-chain of relaxin, and ovarian peptide hormone isolated from ovaries of pregnant sows, has been shown to have the following primary structure: PCA-Ser-Thr-Asn-Asp-Phe-Ile-Lys-Ala-Cys-Gly-Arg-Glu-Leu-Val-Arg-Leu-Trp-Val-Glu-Ile-Cys-Gly-Val-Trp-Ser (2820 daltons). The heterogeneity of relaxin observed during purification procedures is likely to be due to variations in the C-terminal region of the B-chain, in particular the substitution of Gln for Glu20, and the possible addition of arginine or serylarginine at the C terminus. The B-chain exhibited a distribution of sulfhydryl residues relative to one another that is identical to that found in the B-chain of insulin. A similar analogy has already been demonstrated for the A-chains of relaxin and insulin.

Published
1976

27. [23] Sequencing of peptides with dipeptidyl aminopeptidase I

Author

Paul X. Callahan, Stanley Ellis, and J. Ken McDonald

Subjects
chemistry.chemical_classification, chemistry.chemical_compound, Oligopeptide, Dipeptide, chemistry, Arginine, Biochemistry, Cleave, Lysine, Peptide, Asparagine, Pyroglutamic acid
Abstract

Publisher Summary This chapter presents the methodology by which dipeptidyl aminopeptidase I (DAP I) can be utilized in a new approach to the sequencing of small amounts (0.5 μmole or less) of peptides. The ability of DAP I to remove dipeptides, in sequence, from the NH 2 termini of oligopeptides can be followed, for at least several dipeptide products, by time-course chromatography. Although often this is insufficient for establishing sequence, it is possible to modify the peptide substrate in such a way that DAP I generate the alternate, overlapping dipeptides––an advantage not possible with monoaminoacyl aminopeptidases. Certain advantages over chemical methods of sequencing are inherent in this approach. Asparagine and glutamine are recovered as such (not as aspartic or glutamic acid), and there is no tendency to form pyroglutamic acid, as occurs with chemical methods. The inability of DAP I to remove dipeptides with an NH 2 -terminal arginine or lysine is not a problem if the peptide substrates are derived from tryptic digests wherein most, if not all, lysines and arginines are COOH terminal. A limitation arises from the inability of DAP I to cleave the bond on either side of proline. The chapter focuses on the separation of the dipeptide products that result from the action of DAP I on oligopeptides, their recognition in mixtures when separation of the dipeptides is unnecessary, and the approaches necessary for the reordering of those dipeptide products.

Published
1972
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28. Third International Congress of Histochemistry and Cytochemistry

Author

J. E. Kephart, Zenon Steplewski, Kokichi Kanazawa, F. Cisotti, M. P. Ehrlich, K. Holubar, D. F. Swaab, Erich Künzel, J. Thomas Danzi, Erna Avrin, L. Konopska, B. Korych, M. T. Tchaika, Donald W. Misch, Peter W. Neurath, M. M. Coombs, N. H. Bass, Gianfranco Ballare, J. D. Vigario, A. Tixier-Vidal, J. W. Anderson, Peter H. Bartels, Floyd E. Bloom, J. M. S. Prewitt, W. Gössner, V. D. Novikov, Masanori Takeda, A. S. Vecher, Gunter F. Bahr, A. Stammler, Ellen M. Rasch, R. Thalmann, Vick Williams, Lois W. Tice, N. T. Raikhlin, Torbjörn Caspersson, Gianmario Mariuzzi, M. M. Salpeter, Jacques Lipetz, Franca Porcelli, V. Preto Parvis, P. B. Gahan, Hans-Jürgen Herrmann, Karoly Balogh, F. L. Schuster, Z. Lojda, Frederick T. Zugibe, B. Hershenov, Moshe Kalina, Heinz Von Mayersbach, Gordon L. Rosene, C. C. Orton, Jan Wieckowski, M. P. King, Charles E. Hughes, A. L. Bastos, A. A. Castellani, E. E. McGarry, G. Szegly, George L. Wied, Lawrence S. Hurwitz, Jerome P. Horwitz, L. K. Sharashidze, George B. Koelle, Sin Hang Lee, G. C. Budd, Gerhard Müller, A. Björklund, Hilde E. Hirsch, Carlo Alberto Beltrami, R. Håkanson, L. D. Lukyanova, G. G. Glenner, J. Drukker, M. Z. M. Ibrahim, Doina Onicescu, Cornelia Prundeanu, N. V. Samosudova, J. A. F. Silva, S. O. Enenko, C. Pilgrim, Takaharu Matsumoto, Masa-Oki Yamada, Allen Costoff, Peter V. Moulder, F. Patocka, P. Tournier, Bo Thorell, Alberto Candiotti, Vinci Mizuhira, Carl Ritter, A. Simard, Donald R. Hodges, S. Guha, M. I. Parfanovich, D. Bootsma, Wesley J. Birge, J. Hartman, Lloyd J. Roth, Sidney Goldfischer, Blake W. Moore, R. Rigler, M. Rizzotti, M. S. Aksyutina, Lucien J. Rubinstein, William J. Dougherty, V. R. Switsur, Richard M. Torack, B. Perry, Paul J. McMillan, Hélio B. Coutinho, B. Ehinger, Leonard F. Bélanger, K. H. Jaeger, O. Macovschi, D. Zaccheo, Stefan Hovmark, Andre Gerard, Robert S. Ledley, Ferdinando Rossi, R. J. Barrnett, Herbert A. Lubs, J. E. Jirasek, Harold Koenig, M. Stroun, B. Sylvén, V. D. Arutyunov, Richard L. Tyndall, Elisabeth Von der Muehll, X. Yataganas, Brian H. Mayall, J. C. Liu, A. Pope, P. X. Callahan, Susan P. Gaffney, Ei-ichi Yokomura, E. A. Kirianova, L. Monus, Fritz Ruch, Josef V. Freisler, A. M. Terrinha, A. Heller, B. Gabara, Peter J. Stoward, David S. Alkek, G. Kiefer, Alfredo Mariano Garcia, H. H. Hess, Gottfried Werner, Alessandra Forni, Josef Vittek, G. A. Jurzina, P. E. Norgren, H. G. Goslar, Ulrich Welsch, Margaret C. Boadle, Katsumi Wakabayashi, Jean McLean, P. Grigoriadis, Jean R. Adams, C. Bode, M. M. Ogieveckaja, Joseph Rigatuso, Tadao Takeuchi, John E. Pauly, Kendall Preston, Patricia D. Wilson, A. G. E. Pearse, David M. Maeir, T. Abe, O. S. Frankfurt, Jan L. E. Ericsson, Karel Philippens, Gy. Vadasz, E. T. Angelakos, F. Hernández, Frank H. Ruddle, Sally B. Fand, Richard Heitsch, Hideo Takamatsu, M. Matsuda, L. Ya. Yablonovskaya, Wiecher H. VanHouten, Hildegard E. Enesco, I. Törö, Takanori Amakawa, T. J. Conway, M. J. Olszewska, V. E. Shungskaya, Joh. Koudstaal, R. S. Morgan, C. Vladescu, Boris Gueft, A. Urano, Viviane Maggi, Totada R. Shantha, Nicolas Zenker, Lawrence E. Scheving, A. Goldstone, E. N. Sarch, Dean E. Abrahamson, K. Felgenhauer, Thomas B. Shows, J. P. Mitchell, Jeffrey P. Chang, A. A. Masko, Ovidio Duarte-Escalante, L. Roizin, Klaus Wächtler, Lenore Wagner, C. P. Leblond, M. L. Mendelsohn, L. Luksys, K. C. Tsou, Erik Zeuthen, M. Kazama, Helen P. Sorokin, K. A. Gornak, Jácia T. Rocha, T. H. Schiebler, C. W. Goodwin, L. M. Franks, K. Wolff, Sun K. Song, Bun-Ichi Tamaoki, D. A. Sakharov, W. King Engel, Shinichi Imura, Rachele Alberti, J. Ken McDonald, V. Áubrechtova, Patricia A. Kinnison, Yoshihiro Hamashima, Z. A. Cohn, Stanley Scher, C. E. Grossi, J. Jos, Arline D. Deitch, N. V. Donskikh, J.-E. Edström, E. Bajusz, M. F. Kramer, Seth W. Gilkerson, H. Benoit, M. A. Van Dilla, G. Freytag, G. Aureli, E. J. Dupraw, H. R. Tyagi, A. Jarrett, A. I. Bukhonova, C. A. Squier, B. Daneholt, Sunao Iwata, K. Yokoyama, Giovanni Lanza, Margaret S. Misch, F. Gregoire, M. Kage, Ryuei Maeda, Eleanor Rita Lappano-Colletta, L. A. Kamentsky, S-U. Kim, U. M. Gross, Halina Sierakowska, M. Dauwalder, Patricia L. Haley, Shunta Hirose, Dorothy J. Moore, E. B. Masurovsky, Firoze B. Jungalwala, Walter E. Stumpf, Howard I. Siegel, M. Chyle, C. Balduini, A. L. Shnaper, Kei-Ichi Hirai, R. E. Smith, M. Serban, J. R. Coulter, A.-M. Bullens, Voldemar Vilter, Ph. J. Hoedemaeker, N. I. Tsirelnikov, Ines Mandl, K. I. Predkel, Dwo Lynm, Shigeru Morikawa, L. V. Danilova, Masasuke Akamatsu, J. Bolubasz, J. C. Beck, Amour F. Liber, Hans-Georg Schiemer, Peter F. Schatzki, J. D. Elema, J. Bernsohn, N. A. Probatova, Barbara Penar, Masando Hayashi, Tibor Barka, G. Gahrton, Annunzia Fraschini, U. Filotto, Paul F. Doolin, G. Fabris, Sergei P. Sorokin, Mildred Y. Chang, H. Dariush Fahimi, Mitsuo Sasaki, Nina D. Gracheva, Tinrat Stitnimankarn, T. Adesanya Ige Grillo, Gösta Jonsson, Regina Leske, A. Huszczuk, Sophia Kakari, W. Straus, J. Martinez De Morentin, M. F. Sheff, Frank Wohlrab, Timothy C. Appleton, T. Gilbert Scott, Eric A. Barnard, N. S. Sturua, Maria Popescu, Junichi Totsu, Takuma Saito, Lew Cunningham, Benito Monis, Ch. Owman, L. Ya. Lomakina, Alvin M. Burt, Z. Lodin, Satimaru Seno, K. P. M. Heirwegh, Giuseppe Gerzeli, Elliott F. Osserman, K. Nakashio, E. Brodie, W. Sandritter, M. H. Himes, John Pryse-Davis, R. S. Santti, Benjamin F. Trump, Nencioni T, B. Falck, Shinsuke Kanamura, Benjamin F. Jales, Attila Tanyolac, Konrad Akert, Eugene H. Blackstone, Donald B. Fisher, Theodore Peters, Zay B. Curtis, C. Mittermayer, B. Sporrong, Kazuko Uchida, Mortimer L. Mendelsohn, Daniel S. Friend, Yasuo Kishino, William D. Selles, A. V. Sakharova, Hazel Cheng, R. Daoust, Vernon J. Perez, W. Gepts, Stanley Ellis, Philip Ohringer, S. A. Burnasheva, J. E. Scott, A. Ingrami, M. J. Hardonk, Yvonne Hosannah, Carlton E. Blackwood, Jerome P. Miksche, Ludmila Fotin, S. Matsukawa, Otfried Müller, A. M. Baptista, V. Genta, P. F. Mullaney, Antti U. Arstila, G. Mori, H. Goebell, M. Ya. Subbotin, H. Kim, Niel Wald, E. Pascoe, Harold J. Sobel, Hideo Shindo, Merton Sandler, Richard Cornell, A. Riva, Sten W. Jakobsson, R. G. J. Willighagen, P. Sadauskas, V. J. Desmet, Roy O. Weller, Bjarne Pearson, L. Kalevi Korhonen, J. P. Waterhouse, Bernard Droz, Frank S. LaBella, H. Galjaard, C. L. Rosales, Andrzej Vorbrodt, Gerard M. Lehrer, Barry W. Wilson, Maria Gabriella, Stanley G. Sawicki, P. Leth Jørgensen, Nobuo Ohuchi, M. Bradshaw, Ju. J. Tendetnik, S. Virág, Norman G. Anderson, C. Burdick, Alex B. Novikoff, Christopher ’Seinde Adeoye, M. Zamfirescu-Gheorghiu, A. Gropp, K. D. Rokhlenko, H. Ooms, Eli Shuter, J. S. Hugon, V. V. Terskikh, C. Bona, Anne B. Johnson, J. M. Nunes, D. M. Conning, Nobutaka Itoh, S. R. Pelc, Z. Chirulescu, Walter C. Schneider, H. Kobayashi, Sohan L. Manocha, John R. Esterly, Marilyn G. Farquhar, O. E. Rjadneva, J. Lindner, N. G. Stepanova, N. N. Shiukashvili, Russell Ranshaw, A. Schauer, Väinö K. Hopsu-Havu, A. W. Carbonell, George B. Jerzy Glass, F. M. Matschinsky, Moshe Wolman, Edgar E. Smith, P. Satir, Claudia Joandrea-Casian, J. Tappeiner, Hans E. Kaiser, Fran Morriss, K. Grasedyck, J. F. Jongkind, Murray B. Bornstein, Winifred W. Doane, K. D. Eristawi, Giovanni Prenna, L. Matturri, Alexander M. Rutenburg, J. R. Garrett, J. Svejda, Muneaki Abe, B. Lederer, Waine C. Johnson, F. W. D. Rost, J. M. Hewitt, K. P. Ganina, Judith M. S. Prewitt, M. B. Kalamkarova, Robert M. Rosenbaum, Sheldon C. Sommers, Alfred C. Standen, W. G. Whaley, A. V. Zelenin, Paul K. Nakane, N. R. Ringertz, Robert Lev, L. L. Fadeeva, J. De Groote, Jacob S. Hanker, N. N. Sokolov, Jürgen Schlüns, V. I. Malyuk, William Bennett, Italo Nenci, E. O. Riecken, Milan R. Henzl, J. P. Fouquet, Vincent Spitaleri, Frank H. Moyer, T. John Leppi, P. Anker, Chandicharan Deb, Tomichi Masuya, L. Bolund, H. G. Godlewski, A. M. Souza Toledo, Jacques de Graef, Robert Katzman, David Glick, Eli Robins, Horst Zimmermann, Premysl Fric, P. J. Melnick, R. Nayak, S. Stroman, C. W. M. Adams, Charles A. Ashley, Teresa I. Mercado, Margaret E. Long, L. Glismann, D. J. Marshall, C. Velican, Gy. Rappay, Falls B. Hershey, M. Bergeron, A. S. Petrova, Ian T. Young, V. N. Reshetnikov, M. van der Ploeg, I. Diculescu, M. G. Manfredi Romanini, Godfrey C. Hoskins, Henri G. Vetter, Maurice Sandler, Takayuki Harada, E. Bacsy, Robert C. Allen, A. J. Hale, O. I. Epifanova, Geoffrey H. Bourne, Hisao Yamaguchi, Antti Penttilä, P. van Duijn, K. D. Barron, Michio Yamamoto, Georg W. Kreutzberg, D. S. Van Fleet, Akira Mizutani, William H. Fishman, Irmin Sternlieb, Thomas H. Roderick, M. R. Murray, G. Johannes, Theodore A. Wilcox, L. Silverman, J. W. Fischbein, A. H. Koeppen, N. O. Jacobsen, B. M. Pollock, E. S. Ruchadse, W. B. Quay, Victor Dubowitz, Janusz Komender, S. I. Zacks, Paul J. Anderson, Annette Herscovics, H. B. Tewari, J. Filkuka, O. K. Langley, W. H. McShan, E. Birch, Philip Pizzolato, Francesco Della Corte, U. A. Gabunia, Eric Holtzman, Yoshihisa Morizono, Nobuo Ihara, L. Vollrath, L. Guerra, Ezio Giacobini, Jose J. Bubis, S. Curri, M. Borgers, C. Vendrely, A. Lageron, A. Weinstock, Morris J. Karnovsky, Arnold Vogt, V. Dabkevcius, P. N. Dean, B. B. Fuchs, McCormick Templeton, M. A. Presnov, E. Thomas, L. P. Lipchina, D. C. Livingston, D. Killander, Maffo Vialli, Doina Velican, M. Guigon, Dante Marques, Paul L. Wolf, L. C. Junqueira, Bette Seamond, Frederick H. Kasten, J. Srajer, Günter Steinbach, H. H. Benitez, J. F. Lhotka, J. Merzel, Arnold M. Seligman, M. P. Viola-Magni, C. L. Rutherford, E. Szabo, R. D. Lillie, N. J. Nadler, Walter Chavin, Masao Yamamura, A. Lauria, Regina O’Brien, F. L. Leites, N. Marcus, Janice Vazquez, Gabriel C. Godman, C. Poort, R. Barer, Friedrich A. O. Eckner, Daniel Roth, Ludwig Sternberger, Ikuo Suesada, and O. N. Berezina

Subjects
0303 health sciences, Pathology, medicine.medical_specialty, biology, 030302 biochemistry & molecular biology, Acridine orange, Acid phosphatase, Chronic gastritis, Intestinal metaplasia, medicine.disease, Small intestine, 03 medical and health sciences, chemistry.chemical_compound, medicine.anatomical_structure, chemistry, International congress, medicine, Cytochemistry, biology.protein, Immunohistochemistry, 030304 developmental biology
Abstract

The tissue distribution of enzymatic activities in intestinal metaplasia stomachs exhibiting chronic gastritis was compared histochemically with that of the small intestine in man.

Published
1968
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29. Third International Congress of Histochemistry and Cytochemistry

Author

P. Tournier, Bo Thorell, F. Cisotti, Nicolas Zenker, M. P. Ehrlich, K. Holubar, Jose J. Bubis, J. Fischbein, Shinichi Imura, S. Curri, Susan P. Gaffney, Ellen M. Rasch, Totada R. Shantha, Lawrence E. Scheving, Hirose Shunta, G. Freytag, U. M. Gross, M. Borgers, G. Fabris, D. A. Sakharov, G. C. Budd, M. F. Kramer, C. Vendrely, A. Lageron, V. K. Hopsu-Havu, A. Weinstock, D. F. Swaab, Arnold Vogt, J. A. F. Silva, J. F. Jongkind, Murray B. Bornstein, B. Lederer, Zay B. Curtis, B. Sporrong, S. O. Enenko, Kazuko Uchida, P. N. Dean, F. W. D. Rost, B. B. Fuchs, M. Kage, M. B. Kalamkarova, Erna Avrin, William Bennett, M. J. Hardonk, K. H. Jaeger, McCormick Templeton, Z. Lojda, M. Chyle, C. A. Squier, M. T. Tchaika, Paul K. Nakane, Firoze B. Jungalwala, O. N. Berezina, Italo Nenci, E. O. Riecken, J. E. Kephart, Zenon Steplewski, Halina Slerakowska, M. M. Coombs, Joandrea-Casian Claudia, L. L. Fadeeva, J. De Groote, Sergei P. Sorokin, M. A. Presnov, Fritz Ruch, Milan R. Henzl, Ellis Stanley, Lloyd J. Roth, Masasuke Akamatsu, Eleanor Rita Lappano-Colletta, J. P. Fouquet, N. I. Tsirelnikov, K. I. Predkel, Dwo Lynm, L. Konopska, R. Rigler, A. Tixier-Vidal, U. Filotto, Paul F. Doolin, G. Gahrton, Junichi Totsu, M. Wolman, L. V. Danilova, Vincent Spitaleri, Takuma Saito, T. Adesanya Ige Grillo, W. Gössner, Katsumi Wakabayashi, J. J. Bubis, E. Thomas, W. Straus, J. Martinez De Morentin, Shinsuke Kanamura, Harold Koenig, P. X. Callahan, A. S. Vecher, Tinrat Stitnimankarn, Eugene H. Blackstone, E. N. Sarch, Dean E. Abrahamson, Thomas B. Shows, J. P. Mitchell, Droz Bernard, Takanori Amakawa, F. Hernández, Frank H. Moyer, Hazel Cheng, R. Daoust, Forni Alessandra, Josef Vittek, F. L. Schuster, Paul L. Wolf, L. C. Junqueira, Bette Seamond, Alex B. Novikoff, Tadao Takeuchi, J. Tappeiner, Abe Muneaki, E. Pascoe, A. M. Rutenburg, Harold J. Sobel, Jean R. Adams, P. Grigoriadis, Patricia D. Wilson, A. G. E. Pearse, A. Pope, Hideo Shindo, Frederick H. Kasten, Heinz Von Mayersbach, Gordon L. Rosene, L. D. Lukyanova, G. G. Glenner, N. H. Bass, K. Nakashio, Gianfranco Ballare, R. Thalmann, George B. Koelle, Jeffre Y. P. Chang, Frank H. Ruddle, John Pryse-Davis, Jerome P. Miksche, R. S. Santti, M. Ya. Subbotin, J. Srajer, Günter Steinbach, Chandicharan Deb, Tomichi Masuya, R. G. J. Willighagen, L. Bolund, H. G. Godlewski, Gerzeli Giuseppe, A. Gropp, Sin Hang Lee, Seth W. Gilkerson, M. A. Van Dilla, C. Burdick, J. D. Vigario, Hilde E. Hirsch, Stanley Ellis, Carlo Alberto Beltrami, Philip Ohringer, Erik Zeuthen, G. Szegly, M. Kazama, Helen P. Sorokin, J. W. Anderson, R. Håkanson, Merton Sandler, O. S. Frankfurt, H. H. Benitez, C. Pilgrim, J. Lindner, Väinö K. Hopsu-Havu, Peter H. Bartels, J. P. Waterhouse, Bernard Droz, Floyd E. Bloom, Masa-Oki Yamada, B. Perry, Paul J. McMillan, Allen Costoff, A. A. Masko, Takaharu Matsumoto, H. Benoit, G. M. Mariuzzi, F. Patocka, Joh. Koudstaal, McDonald J. Ken, J. Ken McDonald, J. M. S. Prewitt, H. R. Tyagi, Hélio B. Coutinho, Rachele Alberti, M. Stroun, E. B. Masurovsky, Jacques Lipetz, V. D. Novikov, G. Gries, Wiecher H. Van Houten, Balogh Kåroly, Patricia L. Haley, O. Macovschi, S-U. Kim, C. Vladescu, I. Törö, V. E. Shungskaya, Wesley J. Birge, Ines Mandl, C. P. Leblond, Wald Niel, Shigeru Morikawa, Dariush H. Fahimi, Anne B. Johnson, J. E. Jirasek, T. H. Schiebler, H. Kobayashi, C. L. Rosales, A. Jarrett, K. Wolff, Nina D. Gracheva, Gösta Jonsson, Hans-Georg Schiemer, Torbjörn Caspersson, K. P. M. Heirwegh, D. Zaccheo, M. M. Salpeter, L. Monus, E. T. Angelakos, Marilyn G. Farquhar, Gy. Vadasz, Franca Porcelli, K. Yokoyama, M. J. Olszewska, H. Koenig, A. L. Shnaper, A. M. Terrinha, L. P. Lipchina, Ryuei Maeda, Ulrich Welsch, Peter J. Stoward, David S. Alkek, Kalevi L. Korhonen, Jan Wieckowski, Mitsuo Sasaki, M. L. Mendelsohn, Maggi Viviane, L. Luksys, Satimaru Seno, A. M. Souza Toledo, Herbert A. Lubs, Josef V. Freisler, Sophia Kakari, C. Mittermayer, N. A. Probatova, Elisabeth Von der Muehll, David M. Maeir, Jan L. E. Ericsson, Karel Philippens, D. C. Livingston, M. Kalina, J. Drukker, L. Ya. Lomakina, Alvin M. Burt, Z. Lodin, J. C. Liu, G. Kiefer, H. G. Goslar, V. Áubrechtova, Patricia A. Kinnison, A. Heller, E. Brodie, Eli Robins, K. C. Tsou, Z. A. Cohn, Stanley Scher, E. Bajusz, Attila Tanyolac, Theodore Peters, Cornell Richard, D. Killander, John E. Pauly, Vernon J. Perez, Maffo Vialli, J. Hartman, K. D. Rokhlenko, H. Ooms, M. Serban, Voldemar Vilter, Margaret C. Boadle, Jean McLean, M. M. Ogieveckaja, C. W. Goodwin, W. Sandritter, M. H. Himes, William D. Selles, A. V. Sakharova, A. Ingrami, A.-M. Bullens, Roy O. Weller, B. Hershenov, Lenore Wagner, Doina Velican, P. B. Gahan, Brian H. Mayall, G. A. Jurzina, Blake W. Moore, P. E. Norgren, Hildegard E. Enesco, Ju. J. Tendetnik, S. Virág, Norman G. Anderson, Carlton E. Blackwood, Annunzia Fraschini, Boris Gueft, A. Goldstone, Mildred Y. Chang, Nobutaka Itoh, Ch. Owman, Della Corte Francesco, Sally B. Fand, M. Guigon, Daniel S. Friend, Howard I. Siegel, T. Gilbert Scott, B. Ehinger, Donald B. Fisher, K. Felgenhauer, J. S. Hugon, Mortimer L. Mendelsohn, Benito Monis, C. Bode, Richard M. Torack, A. Riva, Elliott F. Osserman, A. A. Castellani, A. Simard, Donald R. Hodges, Dante Marques, Leonard F. Bélanger, A. Urano, B. Thorell, Giacobini Ezio, S. A. Burnasheva, A. Schauer, B. Korych, V. V. Terskikh, Klaus Wächtler, S. Guha, M. I. Parfanovich, D. Bootsma, H. Kim, Richard L. Tyndall, N. G. Stepanova, N. N. Shiukashvili, M. Rizzotti, X. Yataganas, J. M. Nunes, M. F. Sheff, Waine C. Johnson, J. E. Scott, Sun K. Song, O‘brien Regina, G. E. Mazza, J. M. Hewitt, Robert M. Rosenbaum, Andre Gerard, Robert S. Ledley, Ferdinando Rossi, Frank S. LaBella, Christopher ’Seinde Adeoye, B. Sylvén, V. D. Arutyunov, Moshe Kalina, Sheldon C. Sommers, P. Sadauskas, Kishino Yasuo, M. Dauwalder, Alfredo Mariano Garcia, H. H. Hess, V. J. Desmet, H. Galjaard, O. E. Rjadneva, Benjamin F. Jales, Ei-ichi Yokomura, L. Roizin, Erich Künzel, J. Thomas Danzi, Peter V. Moulder, Konrad Akert, Moshe Wolman, M. Zamfirescu-Gheorghiu, J. Bolubasz, J. C. Beck, Amour F. Liber, B. Daneholt, Donald W. Misch, Peter W. Neurath, Masanori Takeda, Arline D. Deitch, C. Bona, Alberto Candiotti, Yvonne Hosannah, Sunao Iwata, Giovanni Lanza, Winifred W. Doane, K. D. Eristawi, Giovanni Prenna, P. F. Mullaney, Vinci Mizuhira, Sohan L. Manocha, John R. Esterly, L. Matturri, J. R. Garrett, Sidney Goldfischer, A. Stammler, Antti U. Arstila, George B. Jerzy Glass, A. W. Carbonell, Stefan Hovmark, F. M. Matschinsky, Hans E. Kaiser, K. P. Ganina, L. K. Sharashidze, Judith M. S. Prewitt, Barbara Penar, Edgar E. Smith, A. L. Bastos, Dorothy J. Moore, Gerhard Müller, A. Björklund, E. A. Kirianova, Jürgen Schlüns, Eric A. Barnard, N. S. Sturua, Maria Popescu, Bjarne Pearson, Kokichi Kanazawa, N. N. Sokolov, V. Parvis Preto, G. Mori, Regina Leske, Glick David, V. I. Malyuk, R. J. Barrnett, M. Bradshaw, W. Gepts, Lois W. Tice, N. T. Raikhlin, L. M. Franks, P. Anker, Gerard M. Lehrer, Barry W. Wilson, H. Goebell, Hideo Takamatsu, Jacques de Graef, Frederick T. Zugibe, C. E. Grossi, J. Jos, S. R. Pelc, Z. Chirulescu, E. E. McGarry, George L. Wied, A. I. Bukhonova, Walter C. Schneider, Margaret S. Misch, Lawrence S. Hurwitz, M. Z. M. Ibrahim, Doina Onicescu, N. V. Samosudova, Penttilä Antti, Shuter Eli, Premysl Fric, Sten W. Jakobsson, Frank Wohlrab, M. Matsuda, L. Ya. Yablonovskaya, T. Abe, C. Balduini, R. Nayak, S. Stroman, Masando Hayashi, Tibor Barka, A. Huszczuk, C. W. M. Adams, Margaret E. Long, L. Glismann, K. A. Gornak, Jácia T. Rocha, D. J. Marshall, Nobuo Ohuchi, A. S. Petrova, Yoshihiro Hamashima, Henri G. Vetter, J.-E. Edström, Peter F. Schatzki, E. Bacsy, D. S. Van Fleet, William H. Fishman, J. D. Elema, Annette Herscovics, J. Bernsohn, Williams Vick, L. A. Kamentsky, H. B. Tewari, Walter E. Stumpf, Kei-Ichi Hirai, R. E. Smith, Timothy C. Appleton, Benjamin F. Trump, P. Satir, Nencioni T, B. Falck, Fran Morriss, K. Grasedyck, J. Svejda, Alfred C. Standen, W. G. Whaley, A. V. Zelenin, N. R. Ringertz, Hisao Yamaguchi, Jacob S. Hanker, Cornelia Prundeanu, K. D. Barron, B. Gabara, R. S. Morgan, Michio Yamamoto, G. Aureli, E. J. Dupraw, F. Gregoire, J. R. Coulter, V. N. Reshetnikov, M. van der Ploeg, Irmin Sternlieb, Robert C. Allen, A. J. Hale, O. I. Epifanova, P. van Duijn, Thomas H. Roderick, Georg W. Kreutzberg, Robert Katzman, David Glick, Horst Zimmermann, Tamaoki Bun-Ichis, A. H. Koeppen, Herrmann Hans-Jürgen, M. Bergeron, Joseph Rigatuso, Gottfried Werner, Kendall Preston, Richard Heitsch, T. J. Conway, Ovidio Duarte-Escalante, N. V. Donskikh, Ph. J. Hoedemaeker, N. O. Jacobsen, B. M. Pollock, E. S. Ruchadse, P. Leth Jørgensen, Lew Cunningham, D. M. Conning, Theodore A. Wilcox, L. Silverman, G. F. Bahr, J. W. Fischbein, Ian T. Young, Vorbrodt Andrzej, Geoffrey H. Bourne, W. B. Quay, Victor Dubowitz, Janusz Komender, S. I. Zacks, Akira Mizutani, J. Filkuka, O. K. Langley, W. H. McShan, E. Birch, M. R. Murray, Paul J. Anderson, Philip Pizzolato, Yoshihisa Morizono, U. A. Gabunia, Eric Holtzman, Nobuo Ihara, L. Vollrath, S. Matsukawa, Otfried Müller, A. M. Baptista, V. Genta, L. Guerra, Maria Gabriella, Stanley G. Sawicki, Russell Ranshaw, Robert Lev, T. John Leppi, P. J. Melnick, Morris J. Karnovsky, Charles A. Ashley, Fotin Ludmila, V. Dabkevcius, Teresa I. Mercado, C. Velican, Gy. Rappay, Falls B. Hershey, I. Diculescu, M. G. Manfredi Romanini, Godfrey C. Hoskins, Maurice Sandler, Takayuki Harada, G. Johannes, J. F. Lhotka, J. Merzel, Arnold M. Seligman, M. P. Viola-Magni, C. L. Rutherford, E. Szabo, R. D. Lillie, N. J. Nadler, Walter Chavin, Masao Yamamura, A. Lauria, F. L. Leites, N. Marcus, Janice Vazquez, Gabriel C. Godman, C. Poort, R. Barer, Friedrich A. O. Eckner, Daniel Roth, Ludwig Sternberger, Ikuo Suesada, C. C. Orton, M. P. King, Charles E. Hughes, Jerome P. Horwitz, Ritter Carl, M. S. Aksyutina, Lucien J. Rubinstein, William J. Dougherty, and V. R. Switsur

Subjects
0303 health sciences, 03 medical and health sciences, Chemistry, International congress, 030302 biochemistry & molecular biology, Cytochemistry, Anatomy, 030304 developmental biology
Published
1968
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30. Detection of a lysosomal carboxypeptidase and a lysosomal dipeptidase in highly-purified dipeptidyl aminopeptidase I (cathepsin C) and the elimination of their activities from preparations used to sequence peptides

Author

Benjamin B. Zeitman, J. Ken McDonald, and Stanley Ellis

Subjects
Dipeptidase, Dipeptidases, Hot Temperature, Isoflurophate, Biophysics, Spleen, Carboxypeptidases, Biochemistry, Chromatography, DEAE-Cellulose, Cathepsin C, medicine, Animals, Molecular Biology, Edetic Acid, chemistry.chemical_classification, biology, Angiotensin II, Hydrolysis, Dipeptidyl Aminopeptidase I, Cell Biology, Lysosomal dipeptidase, Molecular biology, Carboxypeptidase, Cathepsins, medicine.anatomical_structure, Enzyme, chemistry, Liver, Ammonium Sulfate, Rat liver, biology.protein, Chromatography, Gel, Cattle, Chromatography, Thin Layer, Lysosomes
Abstract

Description of the properties of a carboxypeptidase, termed 'catheptic carboxypeptidase C,' and a dipeptidase, termed 'Ser-Met dipeptidase.' Both were found in highly purified DAP I from either beef spleen or rat liver. Methods are described for the removal or selective inactivation of these contaminating enzymes.

Published
1972

31. Cathepsin C: a chloride-requiring enzyme

Author

J. Ken McDonald, Thomas J. Reilly, Stanley Ellis, and Benjamin B. Zeitman

Subjects
Biophysics, In Vitro Techniques, Naphthalenes, Biochemistry, Chloride, Cathepsin C, Hydrolysis, Chlorides, medicine, Organic chemistry, Animals, Anilides, Molecular Biology, chemistry.chemical_classification, biology, Chemistry, Tissue Extracts, Cell Biology, Cathepsins, Enzyme assay, Rats, Enzyme, biology.protein, Spleen, medicine.drug
Published
1966

32. GLUCOSE CATABOLISM IN THE ERGOT FUNGUS, CLAVICEPS PURPUREA

Author

Vernon H. Cheldelin, J. Ken McDonald, and Tsoo E. King

Subjects
Glucose catabolism, Biochemistry, Ergot Fungus, Articles, Biology, Claviceps purpurea, biology.organism_classification, Molecular Biology, Microbiology
Published
1960

33. [22] Preparation and specificity of dipeptidyl aminopeptidase I

Author

J. Ken McDonald, Stanley Ellis, and Paul X. Callahan

Subjects
chemistry.chemical_classification, Substrate Specificities, Dipeptide, Stereochemistry, Dipeptidyl Aminopeptidase I, Substrate (chemistry), Chloride, chemistry.chemical_compound, Enzyme, chemistry, Biochemistry, Reagent, medicine, Side chain, medicine.drug
Abstract

Publisher Summary The dipeptidyl aminopeptidases (DAP) are enzymes that catalyze the consecutive removal of dipeptide moieties from the unsubstituted NH 2 termini of polypeptide chains. Four such enzymes are characterized and shown to have distinctive substrate specificities. Within this group, dipeptidyl aminopeptidase I (DAP I) exhibits the broadest substrate specificity. When DAP I is observed in bovine pituitary extracts, it is characterized as a sulfhydryl-dependent Ser-Tyr-β-naphthylamidase with an absolute or near-absolute chloride requirement and a pH 4 optimum. The purification serves as the basis for the preparation of DAP I. The practicability of using DAP I as a sequencing reagent is greatly enhanced by the relative ease with which a suitable preparation can be made. The broad substrate specificity of DAP I is first observed with β-corticotropin used as a substrate. DAP I activity has also been measured on Gly-Phe-NH 2 . An analysis of the specific bonds cleaved in polypeptide substrates revealed that DAP I can remove dipeptides having penultimate residues with both hydrophilic and hydrophobic side chains.

Published
1972
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34. Separation and identification of dipeptides by paper and column chromatography

Author

J. Ken McDonald, Stanley Ellis, Judith A. Shepard, Paul X. Callahan, and Thomas J. Reilly

Subjects
Chromatography, Autoanalysis, Time Factors, Formates, Chemistry, Elution, Chromatography, Paper, Biophysics, Analytical chemistry, Cell Biology, Dipeptides, Acetates, Biochemistry, Quaternary Ammonium Compounds, Paper chromatography, Column chromatography, Alcohols, Hydroxides, Methods, Solvents, Indicators and Reagents, Amino Acids, Molecular Biology
Abstract

Dipeptides separation and identification by column and paper chromatography for elution times prediction and sequence studies

Published
1970

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