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305 results on '"Petersen, Torben E."'

9. Structural basis for mammalian vitamin [B.sub.12] transport by transcobalamin

Author

Wuerges, Jochen, Garau, Gianpiero, Geremia, Silvano, Fedosov, Sergey N., Petersen, Torben E., and Randaccio, Lucio

Subjects
Vitamin B12 -- Dosage and administration, Brucellosis in cattle -- Care and treatment, Crystals -- Structure, Crystals -- Research, Science and technology
Abstract

Cobalamin (Cbl, vitamin [B.sub.12]) serves for two essential cofactors in mammals. The pathway for its intestinal absorption, plasma transport, and cellular uptake uses cell surface receptors and three Cbl-transporting proteins, haptocorrin, intrinsic factor, and transcobalamin (TC). We present the structure determination of a member of the mammalian Cbl-transporter family. The crystal structures of recombinant human and bovine holo-TCs reveal a two-domain architecture, with an N-terminal [[alpha].sub.6]-[[alpha].sub.6] barrel and a smaller C-terminal domain. One Cbl molecule in base-on conformation is buried inside the domain interface. Structural data combined with previous binding assays indicate a domain motion in the first step of Cbl binding. In a second step, the weakly coordinated ligand [H.sub.2]O at the upper axial side of added [H.sub.2]O-Cbl is displaced by a histidine residue of the [[alpha].sub.6]-[[alpha].sub.6] barrel. Analysis of amino acid conservation on TC's surface in orthologous proteins suggests the location of the TC-receptor-recognition site in an extended region on the [[alpha].sub.6]-[[alpha].sub.6] barrel. The TC structure allows for the mapping of sites of amino acid variation due to polymorphisms of the human TC gene. Structural information is used to predict the overall fold of haptocorrin and intrinsic factor and permits a rational approach to the design of new Cbl-based bioconjugates for diagnostic or therapeutic drug delivery. cobalamin | crystal structure | P259R polymorphism | transport protein

Published
2006

11. Kinetic and structural characterization of a two-domain streptokinase: dissection of domain functionality

Author

Johnsen, Laust B., Rasmussen, Lone K., Petersen, Torben E., Etzerodt, Michael, and Fedosov, Sergey N.

Subjects
Mammals -- Physiological aspects, Streptokinase -- Physiological aspects, Microbial enzymes -- Physiological aspects, Plasminogen activators -- Physiological aspects, Biological sciences, Chemistry
Abstract

Kinetic and structural characterization has been carried out in a two-domain streptokinase from Streptococcus uberis using dissection of domain functionality. Plasminogen (Pg) activation mediated by two recombinant fragments and the N terminal-modified fusion protein has been characterized. From kinetic data it can be seen that one of the fragments, without the gamma domain, could bring on virgin enzymatic activity in bovine Pg

Published
2000

12. Functional analyses of two cellular binding domains of bovine lactadherin

Author

Andersen, Mikkel H., Graversen, Helle, Fedosov, Sergey N., Petersen, Torben E., and Rasmussen, Jan T.

Subjects
Biochemistry -- Research, Glycoproteins -- Research, Cells -- Analysis, Biological sciences, Chemistry
Abstract

Research has been conducted on the glycoprotein bovine lactadherin. The investigation of the interactions between lactadherin and mammalian cell types has been carried out.

Published
2000

13. A refined kinetic analysis of plasminogen activation by recombinant bovine tissue-type plasminogen activator indicates two interconvertible activator forms

Author

Johnsen, Laust B., Ravn, Peter, Berglund, Lars, Petersen, Torben e., Rasmussen, Lone K., Heegaard, Christian W., Rasmussen, Jan, T., Benfeldt, Connie, and Fedosov, Sergey, N.

Subjects
Tissue plasminogen activator -- Research, Biochemistry -- Research, Biological sciences, Chemistry
Abstract

Bovine tissue-type plasminogen activator (tPA) has been heterologously expressed in the Pichia pastoris methylotrophic yeast and characterized. The study showed the presence of two interconvertible forms of recombinant bovine tPA, with only the minor form able to bind and active plasminogen. The single-chain tPA was activated by fibrinogen fragments because of preferential binding.

Published
1998

14. An ester bond linking a fragment of a serine proteinase to its serpin inhibitor

Author

Egelund, Rikke, Rodenburg, Kees W., Andreasen, Peter A., Rasmussen, Margit S., Guldberg, Roy E., and Petersen, Torben E.

Subjects
Esters -- Physiological aspects, Serine -- Physiological aspects, Glycoproteins -- Physiological aspects, Enzyme inhibitors -- Physiological aspects, Chemical bonds -- Physiological aspects, Biological sciences, Chemistry
Abstract

The interaction between the active site of a serine proteinase and the P1-P1' peptide bond of the serpin was analyzed. A direct protein chemical approach was utilized to characterize this association. In addition, the complex between the serine proteinase urokinase-type plasminogen activator and the serpin plasminogen activator inhibitor-1 was subjected to proteolytic digestion under nondenaturing conditions. Results showed that there is an ester bond linking a fragment of the serine proteinase to its serpin inhibitor.

Published
1998

16. MPSA abstracts

Author

Aminlari, Mahmoud, Asquith, Thomas, Sarlo, Katherine, Bailey, Jerome M., Tu, Oanh, Issai, Gilbert, Ha, Alice, Shively, John E., Bell, Alexander W., Baur, Nicole C., Bergeron, John J. M., Ou, Wei -Jia, Thomas, David Y., Cianflone, Katherine, Baldo, Allain, Hincke, Maxwell T., Momparler, Richard L., Laliberté, Josée, Thomson, David M. P., Sutherland, M., Besada, Vladimir, Gonzalez, Javier, Padron, Gabriel, Garay, Hilda, Reyes, Osvaldo, Takao, Toshifumi, Shimonishi, Yasutsugu, Bischoff, Rainer, Roecklin, Dominique, Bouchon, Bernadette, Klarskov, Klaus, Van Dorsselaer, Alain, Brake, Patricia G., Pacitti, Anne, Higgins, Terry, Stevis, Panos, Malinowski, John, McElhiney, Sue, Huang, Janes, Vestal, Christine, Buckel, Scott D., Stevenson, Tracy, Loo, Joseph A., Caffrey, Martin, Wang, Jin, Wallace, Carmichael J. A., Clark-Lewis, Ian, Carraway, C. A. Carothers, Huang, J., Li, Y., Juang, S. -H., Gallo, A., Mayer, B. J., Carraway, K. L., Coleman, Patrick L., Sarpong, Daniel, Deerfield, II, David W., Holland-Minkley, Amanda, Hempel, John D., Nicholas, Jr., Hugh B., Denslow, Nancy D., Folmar, Leroy C., Sullivan, Craig V., Dixon, James D., Mark, Jonathan P., Elicone, Christopher P., Maleknia, Simin D., McGuinness, Brian F., Regnier, Fred E., Afeyan, Noubar B., Dolence, Julia M., Poulter, C. Dale, Egorov, Tsezi, Musolyamov, Alexander, Popineau, Yves, Andersen, Jens, Roepstorff, Peter, Falkenstein, Roberto J., Biscoglio de Jiménez Bonino, Mirtha J., Peña, Clara, Gauggel, D. L., Asquith, T. N., Isfort, R. J., Miller, N. S., Cody, D. B., Giblin, Michael F., Wong, Tuck C., Quinn, Thomas P., Grant, Gregory A., Crankshaw, Mark W., Griffith, Scott, Schroeder, Steve, Quinn, Thomas, Guinet, F., Petillot, Y., Chapsal, J. M., Dubayle, J., Greco, F., Barge, O., Forest, E., Valentin, C., Hahn, Frederick M, Baker, Jonathan A., Poulter, C. Dale, Haniu, Mitsuru, Kenney, William C., Rohde, Michael F., Harman, James G., Lee, Eun Ju, Glasgow, Joel, Lew, Sew Fen, Belduz, Ali O., Harris, Reed J., Molony, Michael S., Keyt, Lene H., Wu, Shiaw -Lin, Hawke, David H., Tso, Jaqueline, Early, Sherrell, Miller, Chad G., Hayman, G. Thomas, Miernyk, Jan A., Hellman, Ulf, Wernstedt, Christer, Góñez, Jorge, Hess, Daniel, Studer, Ralph, Hunziker, Peter E., Hirano, Hisashi, Watanabe, Yoshihiro, Barbashov, Sergei F., Komatsu, Setsuko, Hemmings, Andrew M., Miyagi, Masaru, Tsunasawa, Susumu, Huber, Reuben E., Roth, Nathan J., Gaunt, Michael T., Jenö, Paul, Mini, Thierry, Moes, Suzette, Horst, Martin, Jinnai, Kenji, Ashizawa, Tetsuo, Atassi, M. Zouhair, Johnsen, Anders H., Jensen, Hanne, Rehfeld, Jens F., Kamo, Masaharu, Kawakami, Takao, Miyatake, Norifumi, Tsugita, Akira, Keen, JN, Zagalsky, PF, Findlay, JBC, Kraft, Regine, Kostka, Susanne, Hartmann, Enno, Krutzsch, Henry C., Inman, John K., Machalinski, Claudia, Bonino, Mirtha Biscoglio de Jiménez, McRorie, Donald K., Dieckmann, Gregg R., Heilman, Susan, DeGrado, William F., Pecoraro, Vincent L., Kenny, James, Sahakian, Julie, Tso, Jacqueline, Moyer, Mary B., Burkhart, William A., Muranova, Tatyana, Makova, Lubov, Nicholas, Hugh, Hempel, John, Hinich, Amy, Deerfield, David, Behrmann, Joseph, Ropelewski, Alex, Nixon, Lori, Maneri, Leonard, Nugent, Kerry, Stoney, Ken, Wieser, John, Ohguro, Hiroshi, Palczewski, Krzysztof, Walsh, Kenneth A., Johnson, Richard S., Packman, Leonard C, Webster, Carl, Gray, John, Padrón, G., Morera, V., González, L. J., Támbara, Y., Besada, V., Villalonga, R., Chinea, G., Reyes, O., Bringas, H. Garay R., Nazábal, C., Parkinson, Bruce P., Yamada, Kent A., Randolph, Anne, Pisano, Anthony, Packer, Nicole H., Redmond, John W., Williams, Keith L., Gooley, Andrew A., Rasmussen, Hanne H., Mørtz, Ejvind, Mann, Matthias, Celis, Julio E., Rasmussen, Lone K., Sørensen, Esben S., Petersen, Torben E., Gliemann, Jørgen, Jensen, Poul Henning, Renlund, Staffan, Wadensten, Henrik, Persson, Annika, Persson, Per, Johansson, Agneta, Edlund, Per -Olof, Rose, Donald J., Sack, Ragna, Apffel, Alex, Miller, Chad, Levine, Rodney L., Sakaguchi, Kazuyasu, Zambrano, Nicola, Lewis, Marc S., Baldwin, Eric T., Shapiro, Bruce A., Erickson, John W, Omichinski, James G., Clore, G. Marius, Gronenborn, Angela M., Appella, Ettore, Schröder, Werner, Moser, Irmgard, Pansegrau, Werner, Lanka, Erich, Simpson, Richard J., Eddes, James, Ji, Hong, Reid, Gavin E., Moritz, Robert L., Højrup, Peter, Speicher, David W., Reim, David F., Speicher, Kaye D., Srinivasa, B. R., Barde, S. P., Stirtan, William G., Sukhanova, Alyona, Vorob'ev, Sergey, Gabibov, Alexander, Bronstein, Igor, Tanaka, Kenji, Einaga, Kuniko, Tsukada, Minoru, Tait, Jonathan F., Fujikawa, Kazuo, Takamoto, Keiji, Satake, Kazuo, Vakser, Ilya A., Velikodvorskaia, V. V., Gabibov, A. G., Rabinkov, A. G., Videler, Tennie, Osborne, Michael, Moore, Geoffrey, James, Richard, Kleanthous, Colin, Walent, Jane H., Bessen, Richard, Marsh, Dick, Clore, G. Marius, Niece, Ronald L., Tsao, Francis H. C., Wang, Hong, Weinberger, Scot R., Chakel, Lynn M., Wondrak, Ewald M., Kimmel, Alan R., and Louis, John M.

Published
1994
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18. Binding of cobalamin and cobinamide to transcobalamin from bovine milk

Author

Fedosov, Sergey N., Petersen, Torben E., and Nexo, Ebba

Subjects
Ligand binding (Biochemistry) -- Research, Vitamin B12 -- Research, Chemical reaction, Rate of -- Research, Biological sciences, Chemistry
Abstract

A study of the reaction between ligands cobalamin (Cbl) and cobinamide (Cbi) and Cbl-depleted transcobalamin (TC) from bovine milk was conducted to examine the binding characteristics of the ligands. The individual rate constants both for TC + Cbl associated and for TC-Cbl dissociation were derived. The binding of an analogue (Cbi) to TC was 20 times slower and its release from the complex TC-Cbi occurred 230 times faster than Cbl. Variations in the affinity of Cbl and Cbi to TC, particularly at the ligand liberation process, were also observed.

Published
1995

26. Composite organization of the cobalamin binding and cubilin recognition sites of intrinsic factor

Author

Fedosov, Sergey N., Fedosova, Natalya U., Berglund, Lars, Moestrup, Soren K., Nexo, Ebba, and Petersen, Torben E.

Subjects
Ligand binding (Biochemistry) -- Research, Radioligand assay -- Research, Vitamin B12 -- Atomic properties, Vitamin B12 -- Research, Biological sciences, Chemistry
Abstract

The binding of cobalamin (Cbl) to intrinsic factor (IF150) and its fragments, assembly of the IF domains in the presence of Cbl and interaction of the IF variants with cubilin are determined. The parameters obtained for ligand and receptor binding indicate that both full-length IF150 and the fragments might be involved in Cbl assimilation.

Published
2005

27. Assembly of the intrinsic factor domains and oligomerization of the protein in the presence of cobalamin

Author

Ferdosov, Sergey N., Fedosova, Natalya U., Berglund, Lars, Moestrup, Soren K., Nexo, Ebba, and Petersen, Torben E.

Subjects
Oligomers -- Research, Intrinsic factor (Physiology) -- Research, Vitamin B12 -- Research, Vitamin B12 metabolism -- Research, Biological sciences, Chemistry
Abstract

The cobalamin (Cbl)-induced oliigomerization of recombinant human intrinsic factor (IF) is presented. Cbl saturated protein was separated by gel filtration into peaks I and II, which contained according to SDS electrophoresis the 50 kDa full-length protein IF(sub 50) and a mixture of two fragments, respectively.

Published
2004

28. PP3 forms stable tetrameric structures through hydrophobic interactions via the C-terminal amphipathic helix and undergoes reversible thermal dissociation and denaturation

Author

Pedersen, Lise R L, Nielsen, Søren Bang, Hansted, Jon Gade, Petersen, Torben E, Otzen, Daniel E, and Sørensen, Esben S

Abstract

The milk protein proteose peptone component 3 (PP3), also called lactophorin, is a small phosphoglycoprotein that is expressed exclusively in lactating mammary tissue. The C-terminal part of the protein contains an amphipathic helix, which, upon proteolytic liberation, shows antibacterial activity. Previous studies indicate that PP3 forms multimeric structures and inhibits lipolysis in milk. PP3 is the principal component of the proteose peptone fraction of milk. This fraction is obtained by heating and acidifying skimmed milk, and in the dairy industry milk products are also typically exposed to treatments such as pasteurization, which potentially could result in irreversible denaturation and inactivation of bioactive components. We show here, by the use of CD, that PP3 undergoes reversible thermal denaturation and that the α-helical structure of PP3 remains stable even at gastric pH levels. This suggests that the secondary structure survives treatment during the purification and possibly some of the industrial processing of milk. Finally, asymmetric flow field-flow fractionation and multi-angle light scattering reveal that PP3 forms a rather stable tetrameric complex, which dissociates and unfolds in guanidinium chloride. The cooperative unfolding of PP3 was completely removed by the surfactant n-dodecyl-β-d-maltoside and by oleic acid. We interpret this to mean that the PP3 monomers associate through hydrophobic interactions via the hydrophobic surface of the amphipathic helix. These observations suggest that PP3 tetramers act as reservoirs of PP3 molecules, which in the monomeric state may stabilize the milk fat globule. Structured digital abstract • PP3 and PP3 bind by circular dichroism (View interaction) • PP3 and PP3 bind by molecular sieving (View interaction) • PP3 and PP3 bind by fluorescence technology (View interaction) • PP3 and PP3 bind by molecular sieving (View interaction).

Published
2012

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