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1. Changes in Immunospecificity and Biologic Activity of Bovine Insulin Due to Subsequent Removal of the Amino Acids B1, B2 and B3

Author

L. Kerp, H. Kasemir, H. R. Henrichs, R. Geiger, J Han, and S. Steinhilber

Subjects
medicine.medical_specialty, Chemical Phenomena, Phenylalanine, Endocrinology, Diabetes and Metabolism, medicine.medical_treatment, Guinea Pigs, Blood sugar, Adipose tissue, Antibodies, Iodine Radioisotopes, Epitopes, Structure-Activity Relationship, Glutamates, In vivo, Internal medicine, Internal Medicine, medicine, Animals, Insulin, Amino Acid Sequence, Amino Acids, Bovine insulin, chemistry.chemical_classification, biology, Chemistry, Valine, Carbon Dioxide, In vitro, Amino acid, Kinetics, Endocrinology, Adipose Tissue, Immunologic Techniques, biology.protein, Cattle, Binding Sites, Antibody, Antibody, Peptides, Ultracentrifugation
Abstract

The influence of splitting off the N-terminal amino acids B1, B2 and B3 of bovine insulin on the binding of these derivatives to antibodies raised with bovine insulin in guinea pigs and on biologic insulin activities is investigated. In comparison with bovine insulin the standard free energies −ΔF°1 for complex formation between high affinity antibodies Ak1 and des-PheB1-insulin or des-(Phe-Val)B1-2-insulin are reduced to 77 per cent and 76.3 per cent respectively, with a further decrease to 68 per cent for des-(Phe-Val-Asn)B1-3-[PyrB4] insulin. The standard free energy -ΔF°2 for complex formation between low affinity antibodies Ak2 and des-PheB1-insulin drops to 48.4 per cent. Further splitting off of the N-terminal amino acids B2 and B3 completely abolishes the antigen binding to Ak2. The ability of both des-PheB1-insulin and des-(Phe-Val)B1-2-insulin to lower the in vivo blood sugar level does not differ significantly from bovine insulin, whereas the in vivo activity of des-(Phe-Val-Asn)B1-3-[PyrB4] insulin decreases to 70±7 per cent. The in vitro biologic activity, tested on isolated fat cells, is slightly reduced to 89±9 per cent for des-PheB1-insulin, to 86±3 per cent for des-(Phe-Val)B1-2-insulin and to 68±6 per cent for des-(Phe-Val-Asn) B1-3-[PyrB4] insulin.

Published
1974
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2. Fourth Annual Meeting of the European Association for the study of diabetes

Author

M. E. Abrams, D. R. Boyns, J. R. Crossley, R. J. Jarrett, H. Keen, D. Andreani, G. Menzinger, F. Fallucca, A. Alibebti, G. Tamburrane, D. Andreev, S. Ditzov, G. Dashev, D. Strashimirov, A. Appels, B. Willms, H. D. Söling, V. H. Asfeldt, Gh. Bacanu, B. Bakker, F. H. Roerdink, P. R. Bouman, A. Coert, N. M. V. Jaspers, L. Barta, R. Beckmann, W. Berger, A. Beringer, G. Geyer, H. Mösslacher, K. H. Tragl, W. Waldhäusl, J. Beyer, K. Schöffling, H. Ditschuneit, S. Raptis, E. Wolf, E. Güntert, E. F. Pfeiffer, N. Bilic, J. P. Felber, K. Bojanowicz, A. Zubowski, Z. Rybarczyk, C. Bonessa, L. Cremonini, B. Borrebaek, Ø. Spydevold, P. Botterman, P. Dieterle, P. C. Scriba, K. Schwarz, B. J. Boucher, K. Mashiter, L. Stimmler, F. Vince, P. Walters, T. R. Csorba, W. J. H. Butterfield, M. J. Whichelow, A. R. Boyns, R. Mahler, N. Pearce, B. Bruni, V. Büber, J. -P. Felber, A. Vannotti, K. D. Buchanan, J. E. Vance, K. Dinstl, R. H. Williams, B. D. Cox, N. M. Cohen, D. P. Alexander, H. G. Britton, D. A. Nixon, R. A. Parker, L. Cegrell, G. W. Chance, E. C. Albutt, C. Chlouverakis, P. White, N. Juel Christensen, G. Contesse, G. Pathé, J. Crabbé, J. Scarlata, G. Crepaldi, M. Muggeo, A. Tiengo, G. Enzi, G. Federspil, A. Trisotto, A. Czyżyk, A. Gregor, A. Dawidowicz, M. de Gasparo, Che. Malherbe, K. Thomas, J. J. Hoet, I. De Leeuw, M. Dérot, M. Rathery, G. Rosselin, James G. Devlin, Marion Duggan, U. C. Dubach, I. Forgò, R. Fellin, H. Muggeo, S. B. Fagerberg, A. Axelsson, S. Fankhauser, B. Morell, K. Federlin, H. -D. Flad, D. Kriegbaum, D. A. Rivier, E. Fellmann, D. Glaubitt, U. Hönlinger, I. Ulrich, K. Wulff, H. Förster, K. Brauch, H. Mehnert, F. Dittmar, H. Frerichs, W. Creutzfeldt, G. Fbeytag, W. Schabschmidt, G. Klöppel, Denise Friedler, J. P. Benhamou, J. Lubetzki, E. Azerad, A. Gnudi, C. Coscelli, V. Palmari, G. Valenti, U. Btttturini, F. Gomez, L. Guidoux-Grassi, J. Maerki, R. Guidoux, J. J. Groen, D. Grüneklee, H. Liebermeister, W. H. Schilling, H. G. Solbach, L. Herberg, H. Daweke, B. Guy-Grand, M. Tutin, H. Bour, D. R. Hadden, J. M. G. Harley, D. A. D. Montgomery, J. S. Mackay, Lise G. Heding, C. Hellerström, H. Stork, S. Westman, F. H. Schmidt, C. F. Boehringer, Söhne GmbH, Dieter Hepp, David R. Challoner, Robert H. Williams, M. Berger, F. A. Gries, H. Preiss, K. Jahnke, J. B. Herman, A. Keynam, D. M. Hill, A. D. Munro-Faure, J. Anderson, Z. Horn, A. Jakob, R. E. Humbel, U. Buxtorf, E. R. Froesch, N. S. Track, A. Kaeding, H. Karmann, P. Mialhe, H. Kasemir, U. Paulus, S. Steinhilber, L. Kerp, E. M. Kohner, N. W. Oakley, T. Russell Fraser, and J. Kühnau

Subjects
0303 health sciences, medicine.medical_specialty, business.industry, Endocrinology, Diabetes and Metabolism, Association (object-oriented programming), 030209 endocrinology & metabolism, Human physiology, medicine.disease, 03 medical and health sciences, 0302 clinical medicine, Diabetes mellitus, Family medicine, Internal Medicine, Medicine, business, 030304 developmental biology
Published
1968
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3. Seventh Annual Meeting of the European Association for the Study Of Diabetes Southampton, England, September 15–17, 1971 Abstacts, Part 1

Author

H. Bibergeil, W. J. H. Butterfield, F. Fallucca, H. Brunengraber, M. J. Munday, Eveline Eschwège, M. Hinz, J. Rogers, O. Richter, J. Hanoune, B. Jeanrenaud, Kjell Asplund, H. Laube, G. Stirati, G. Ghirlanda, C. Dumitrescu, Aa. Hein Christiansen, I. Pencev, L. Nye, S. Ditzov, Claes Hellerström, L. Bodic, V. Gligore, G. Brooser, I. Mastrogiacomo, K. W. Taylor, R. Franchi, R. Fussgänger, L. Stoichescu, Y. Vierne, B. Charbonnel, L. Sjöström, J. Girard, E. Jéquier, U. Fischer, George E, O. Alpi, G. C. Gazzola, M. Austoni, G. Ballerio, F. K. Jansen, G. Chiumello, G. G. Guidotti, J. G. Mills, L. Baldet, Elizabeth Mayne, S. Munkgaard Rasmussen, G. Tamburrano, P. Zöfel, A. Luyckx, M. Carnelutti, U. Cordes, H. Hommel, J. P. Felber, R. Luft, Aa. Vø und, F. Mira, V. Chabot, I. Calusera, S. Frezzato, J. Guillon, J. Terpstra, R. Michael, Brigitte Ziegler, L. Anghelescu, Ernst-Friedrich Pfeiffer, Aa. Vølund, S. Nistrup Madsen, M. Miclutia, S. E. Brolin, G. Freytag, J. Linde, W. D. Gassel, A. Fernandez-CruzJr., M. Ionesou, W. Creutzfeldt, A. Hegedüs, U. Deuticke, J. B. Attali, J. F. Biebuyck, L. Kerp, Gh. Bacanu, J. J. Connon, H. Fiedler, K. E. Schröder, G. Fedeli, N. Katsilambros, S. K. Varma, K. G. M. M. Alberti, Günter Klöppel, E. Napoli, Margaret J. Whichelow, G. A. Cinotti, B. Bierens de Haan, M. J. del Guercio, B. Bruni, G. Tchobroutsky, G. Perry, N. Mosora, L. Papoz, M. Bolea-Feldman, K. D. Hepp, N. Sicolo, F. A. Gries, G. Cavazzini, A. Fernandes-CruzJr., D. Bal, A. C. Asmal, M. Ziegler, Beyer J, J. Lawecki, D. Grüneklee, H. Daweke, Barbara Rudas, J. J. Turner, B. Schröder, K. D. Buchanan, G. Sell, K. Mylarch, T. Holan, E. Capra, S. Fankhauser, E. O. Baiasse, E. Bruck, C. Creutzfeldt, F. Belfiore, J. M. Warnet, S. Campeami, G. Menzinger, L. Olteanu, K. Bojanowicz, J. A. Weaver, T. Fekete, L. Herberg, O. Wieland, M. Varma, V. Turcanu, John Edwards, F. Gomez, M. Rathery, Y. Abdel Rahman, S. J. H. Ashcroft, C. J. Vardey, T. Deckert, P. Lefebvre, D. Andreani, M. Zaccaria, N. Sieolo, Raimundo Goberna, D. P. M. Howells, D. Andreev, B. Karamanos, F. Nistor, S. W. Cushman, Hung Cheng, J. J. Heindel, G. Piemonte, Jean Franckson, R. R. de Mowbray, W. Guder, B. D. Cox, Etienne Brachet, L. Boquist, W. Stauffacher, T. Beraru, M. Luque Otero, N. Krall, J. Hahn, Ch. Rouiller, L. Sirskov, V. Maier, L. Orci, C. Lopiz-Quijada, C. Coscelli, W. G. Whyte, W. Rippel, V. Büber, J. Fövenyi, A. Gnudi, V. Palmari, R. K. Blach, P. W. Adams, J. Iversen, A. J. Valleron, P. Ronchi, H. Rogala, E. Goth, Niels Juel Christensen, J. G. Devlin, U. Keller, H. Keen, R. Leclercq, D. P. Cameron, C. Geldermans, J. Kuti, F. Assimacopoulos, R. A. Jackson, Åke Lernmark, E. Jutzi, N. W. Oakley, H. Schatz, J. P. Aboulker, J. L. Richard, L. Campeanu, R. A. Bacchus, R. Assan, A. Serban, S. J. Heaney, I. De Leeuw, R. Fenici, R. S. Walker, M. Amherdt, A. Z. Middelheim, D. Casara, L. Lo Vecchio, H. M. J. Krans, J. M. Bassett, L. B. Martin, N. S. Track, J. Sehlin, J. Mirouze, E. Cerasi, George Gross, T. Clausen, R. M. Buckle, A. Aynsley-Green, B. Hellman, U. Advani, D. Pometta, L. Barta, V. V. Pipilian, U. Heink, E. Rattenhuber, R. Arnold, S. Efendic, H. Kaffarnik, Christian Berne, A. Kaeding, S. R. Bloom, S. D. Garner, V. Wynn, C. A. Geser, A. V. Greco, S. Triggs, G. C. Reffo, C. Jafflol, W. J. H. Butterfieid, D. R. Hadden, H. J. Hahn, R. Vanroux, C. De Palo, G. Federspil, L. G. Meade, Henri Ooms, D. Ancreev, Mária Judit Molnár, U. Birk Lauridsen, I. B. Täljedal, P. Björntorp, J. Michl, B. Petersson, A. Czyzyk, R. J. Jarrett, S. Steinhilber, D. R. London, J. R. Scherrer, O. Förster, G. Gambassi, Schöffling K, H. Frerichs, D. A. D. Montgomery, E. Saibene, M. Javicoli, J. Hessing, M. Szadkowski, W. H. Davies, N. Tarkolev, P. J. Randle, C. Scandellari, and E. R. Froesch

Subjects
0303 health sciences, medicine.medical_specialty, business.industry, Endocrinology, Diabetes and Metabolism, 030209 endocrinology & metabolism, Human physiology, medicine.disease, 03 medical and health sciences, 0302 clinical medicine, Family medicine, Diabetes mellitus, Internal Medicine, medicine, Optometry, business, 030304 developmental biology
Published
1971
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4. Second Annual Meeting of the European Association for the Study of Diabetes abstracts

Author

J. T. Ireland, B. K. Patnaik, L. J. P. Duncan, Z. Jaksic, A. Jakob, N. Lauper, R. Flury, A. Labhart, E. R. Froesch, R. J. Jarrett, H. Keen, N. Track, J. Jervell, J. Vallance-Owen, J. S. Bajaj, K. Jørgensen, C. Binder, Aa. V. Nielsen, L. Kammerer, M. Bretán, L. Nemsánszky, L. Jakab, S. Virág, S. Virag, E. Keat, L. Kerp, F. Kieling, S. Steinhilber, L. Keep, B. Knick, R. Korec, W. Korp, L. Lalouschek, R. E. Levett, K. Summer, K. Krentz, M. Kristensen, Friedrich Kuhlencordt, F. Kuhlencordt, J. Kühnau, H. -W. Meyer, A. E. Lambert, J. J. Hoet, L. Lambotte, W. C. Shoemaker, P. Lefebvre, G. Lenti, A. Pellegrini, G. Pagano, M. V. Brotzu, F. Sirigu, H. Lestradet, I. Deschamps, H. Liebermeister, R. Rüenauver, D. Grüneklee, W. Schilling, K. Jahnke, H. Daweke, G. Löffler, K. F. Weinges, C. Lopez-Quijada, J. L. R-Candela, A. Loubatieres, M. M. Mariani, R. Alric, C. Lowy, A. H. Rubenstein, A. D. Weight, T. J. Martin, T. Russell, R. Luft, L. Madison, E. Cerasi, U. S. von Euler, A. Margolis, I. Bugala, L. Marasek, Vincent Marks, P. J. N. Howorth, Ellis Samols, F. C. Greenwood, C. Mazzi, F. Melani, J. Lawecki, K. M. Bartelt, E. F. Pfeiffer, G. Menzinger, F. Fallucca, L. Aliberti, D. Andreani, U. A. Meyer, E. Miki, P. Elliott, R. Milani, M. Bianchessi, J. Mirouze, E. Cartry, F. Saade, C. Jaffiol, P. Montenero, P. Denatone, E. Donatone, H. Ørskov, J. Östman, I. Øye, D. Sinclair, L. F. Pallardo, J. Cartillo-Olivares, J. Guijo, J. M. Garcia Garrido, J. Castillo-Olivares, J. L. Matute, G. Pathe, G. Comtesse, U. Polge, G. Contesse, I. Pavel, R. Pieptes, Jørgen Pedebsen, L. Mølsted Pedersen, K. R. Jørgensen, I. Penchev, G. Piancino, P. P. Martini, C. A. Cravetto, A. Pieri, P. T. Scarpelli, E. Pihl, S. Falkmer, D. Pometta, J. Tatot, S. B. Rees, T. Kuwabara, J. Taton, J. E. Poulsen, A. U. Werner, G. Pozza, A. Ghidoni, E. Sanesi, P. Quinto, O. Flamigni, R. Tirelli, C. Flamingni, Ole J. Rafaelsen, J. Lyngsoe, T. Deckert, Edith Reske-Nielsen, Knud Lundbæk, J. L. Roderiguez-Minon, M. Rosell-Perez, C. J. Hedeskov, V. Esmann, G. Rosselin, G. Tchobroutsky, P. Freychet, R. Assan, M. Derot, Barbara Rudas, H. Liebermeisteb, Matilde Salinas, E. Samols, J. Tyler, V. Marks, V. Schliack, F. Skovborg, J. Schlichtkrull, J. Ditzel, Z. Skrabalo, A. Stavljenic, I. Crepinko, N. Dimitrov, P. H. Sönksen, J. P. Ellis, F. Greenwood, J. D. N. Nabarro, H. D. Söling, R. Zahlten, B. Willms, W. Stauffacher, B. Jeanrenaud, B. Ch. J. Sutter, V. Meyer, P. Mialhe, K. Thomas, M. de Gasparo, D. Toussaint, W. Gepts, G. W. Pickering, J. A. Fraser, L. Travia, L. Dalla Torre, G. Forcina, L. Gandolfo, D. S. Turner, N. McIntyre, M. Tutin, F. Rousselie, M. Rathery, H. Borna, H. Bour, R. H. Unger, L. Recant, M. McGavran, M. D. Siperstein, Ph. Vague, R. Depieds, G. Boeuf, J. L. Codaccioni, J. Vague, P. Vague, A. Vitelli, G. Segre, P. Martino, A. Saiani, P. F. Martini, A. Saisni, S. Vuletic, P. Wahl, W. Kettnaker, W. Walaas, O. Walaas, K. E. Wildenhoff, H. Dalsager, N. Schwartz, M. Böttcher, N. Sakomoto, J. Winand, J. Furnelle, J. Christophe, J. W. Woenckhaus, D. Günter, H. Yde, D. A. B. Young, B. Benson, G. R. Zahnd, A. Luyks, N. Zaragoza, and J. P. Felber

Subjects
medicine.medical_specialty, business.industry, Endocrinology, Diabetes and Metabolism, Family medicine, Association (object-oriented programming), Diabetes mellitus, Public health, Internal Medicine, Medicine, Human physiology, Metabolic disease, business, medicine.disease
Published
1966
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5. Influence of Prednisolone and ACTH on the Formation of Insulin-Binding Antibodies

Author

E. Berning, L. Kerp, S. Steinhilber, Kristen C. Sihler, and S. Raju

Subjects
medicine.medical_specialty, business.industry, Insulin Antibodies, Prednisolone, Insulin, medicine.medical_treatment, Freund's Adjuvant, Guinea Pigs, Immunology, General Medicine, Antigen binding, Iodine Radioisotopes, Endocrinology, Adrenocorticotropic Hormone, Internal medicine, Antibody Formation, medicine, Animals, Immunology and Allergy, Immunization, business, medicine.drug
Published
1967
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6. Localisation of Antibody-binding Sites on Insulin Molecules

Author

L. Kerp, S. Steinhilber, H. Kasemir, and F. Kieling

Subjects
Electrophoresis, Injections, Intradermal, Swine, Insulin Antibodies, medicine.medical_treatment, Immunology, Biology, Text mining, Iodine Isotopes, Diabetes Mellitus, medicine, Animals, Insulin, Immunology and Allergy, Binding Sites, Sheep, business.industry, Immune Sera, General Medicine, Antigen binding, Antibody Formation, Cattle, business, Ultracentrifugation
Published
1969
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8. 3. Kongre� der Deutschen Diabetes-Gesellschaft

Author

A. Appels, B. Willms, H. D. S�ling, F. Bahner, L. Barner, H. Pressler, M. Berger, L. Herberg, F. A. Gries, K. Oberdisse, A. Beringer, K. H. Tragl, H. M�sslacher, B. Sokopp, G. Geyer, W. Waldh�usl, J. Beyer, J. Happ, E. B�hle, K. -E. Schr�der, S. Raptis, R. Boos, K. Salfeld, P. Bottermann, P. Dieterle, K. Schwarz, P. C. Scriba, V. B�ber, J. -P. Felber, K. -H. Dehmel, B. Kraus, H. Kuhlmann, H. Mehnert, H. Ditschuneit, J. -D. Faulhaber, E. N. Petrttzzi, A. Englhardt, H. Preiss, E. G�ttler, K. Jahnke, D. Rivier, N. Zaragoza, G. Freytag, G. Kl�ppel, W. Reichel, P. G�bel, D. Klaus, H. Siebner, W. Gross, R. Kaesmann, D. Gr�neklee, H. Liebermeister, W. H. Schilling, H. G. Solbach, L. Hehberg, H. Daweke, H. Hammerl, Ch. Kr�nzl, G. Nebosis, O. Pichler, M. Studlar, M. Haslbeck, H. F�rster, C. -A. Geser, A. Hasselblatt, W. H. Hauss, G. Junge-H�lsing, I. Kuckulis, H. Otto, J. Rawytsch, H. Wagner, D. Hepp, R. H. Williams, T. Hillmer, H. Frerichs, J. Haller, W. Creutzfeldt, H. H. Hoffmann, H. Schmitt, K. Hubrich, R. Kattermann, E. Kallee, K. Wilms, H. Kasemir, U. Paulus, S. Steinhilber, L. Kerp, H. Kuhlmannn, R. Bindig, H. P. Missmahl, B. M�ller-Oerlinghausen, F. H. Schmidt, U. Schwabe, H. Blaise, L. Bette, Ch. Klein, M. Neubauer, F. Melani, K. Sch�ffling, E. F. Pffeiffer, H. Noelle, J. Althoff, K. Rompel, J. S. Soeldner, U. Plischke, G. Biro, K. F. Weinges, K. E. Schr�der, E. F. Pfeiffer, E. O. Riecken, G. A. Martini, H. Sauer, E. Rojas-Hidalgo, R. Sanwald, E. Ritz, D. Schaps, H. Schmidiinger, H. -F. v. Oldershausen, E. Musch, D. Sinn, H. Stork, K. v. Dahl, Ch. Teuber, D. Sch�n, H. F. v. Oldershausen, W. Vogt, K. Mengel, R. Ebert, J. Kleineke, M. Jellinghaus, C. Helierstr�m, M. Telib, A. Teuscher, R. Auckenthauer, M. Gasser, R. Richterich, L. Weiss, W. Guder, O. Wieland, W. Wigger, I. Stegemann, F. Scheler, W. Creutz-Feldt, P. Ben-Ami, J. W. Woenckhaus, H. Schneller, R. Zahlten, and W. Reimoid

Subjects
0303 health sciences, 03 medical and health sciences, medicine.medical_specialty, 0302 clinical medicine, business.industry, Endocrinology, Diabetes and Metabolism, Family medicine, Internal Medicine, Medicine, 030209 endocrinology & metabolism, Human physiology, business, 030304 developmental biology
Published
1969
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9. Ein Verfahren zum Nachweis insulinbindender Antikörper durch Differentialadsorption

Author

L. Kerp, H. Kasemir, and S. Steinhilber

Subjects
Gynecology, medicine.medical_specialty, business.industry, Drug Discovery, medicine, Molecular Medicine, General Medicine, business, Genetics (clinical)
Abstract

Die beschriebene Methode gestattet es, in einem einfachen und rasch durchzufuhrenden Arbeitsgang die Antikoperaktivitat von Antiinsulinseren zu messen und als Titer anzugeben. Mit der gleichen Technik konnen bei konstanter Proteinkonzentration und steigenden Insulinkonzentrationen Bindungskurven aufgenommen werden, weil sich fur jeden Mespunkt sowohl das freie als auch das proteingebundene Insulin bestimmen lassen. Dadurch ist es moglich, fur isolierte Immunglobuline die Konzentrationen der Antikorperbindungsstellen und die Assoziationskonstanten fur die Insulin-Antikorper-Bindung zu berechnen. Die Fehlerquellen des bisher hierzu angewendeten komplexometrischen Elektrophoreseverfahrens nachBerson u. Mitarb.2, 3 werden diskutiert.

Published
1966
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10. Trennung der Strahlenschädigungsprodukte von Insulin-131J und Untersuchung ihrer Eigenschaften

Author

Kristen C. Sihler, F. Kieling, S. Steinhilber, G. Hoffmann, and L. Kerp

Subjects
Radiology, Nuclear Medicine and imaging, General Medicine
Abstract

ZusammenfassungDurch Gelfiltration von 131J-signiertem Rinderinsulin auf Sephadex G 50 und G 75 können drei radioaktive Hauptkomponenten (I, II und III) scharf voneinander getrennt werden. Die Strahlenschädigungsprodukte I und III neh-men in Abhängigkeit von der spezifischen Aktivität des Insulins und von der Zeit nach der Markierung des Insulins zu. Aus dem Verhalten der Komponenten I, II und III bei der Gelfiltration auf Sephadex, bei der Ultrazentrifugation und der Fällung mit Trichloressigsäure kann geschlossen werden, daß es sich bei I um ein großmolekulares (MG < 150 000, > 70 000) Strahlenschädigungsprodukt, bei II um intaktes Insulin und bei Komponente III um kleinmolekulare Spalt-produkte (MG ~ 600) von Insulinmolekülen handelt. Das intakte Rinderinsulin der Komponente II wird im Gegensatz zu I und III durch spezifische Antikörper gebunden und besitzt biologische Insulinaktivität. Das Verfahren ist geeignet, um intaktes Rinderinsulin-131J, wie es zur immunologischen Insulinbestimmung im Blut und zum Nachweis insulinbindender Antikörper benötigt wird, von strahlen-geschädigtem Insulin zu trennen.

Published
1967
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11. Vergleichende analyse der gegen rinderproinsulin und rinderinsulin gebildeten antikörper

Author

D.D. Schmidt, L. Kerp, and S. Steinhilber

Subjects
medicine.medical_specialty, endocrine system, High affinity binding, endocrine system diseases, medicine.medical_treatment, Biophysics, Biochemistry, Structural Biology, Internal medicine, Genetics, medicine, Binding site, Molecular Biology, Bovine insulin, Proinsulin, Antiserum, medicine.diagnostic_test, biology, Chemistry, Insulin, Cell Biology, Molecular biology, Endocrinology, Immunoassay, biology.protein, Antibody, hormones, hormone substitutes, and hormone antagonists
Abstract

Guinea-pig antisera to bovine insulin and proinsulin were analysed and the association constants and the concentrations of combining sites specific for insulin and for the C-chain were determined. Both antisera contained combining sites with higher (Ak1 sites) and lower (Ak2 sites) affinities for the cross-reacting antigens.Antisera produced in response to both insulin and proinsulin had similar concentrations of both the more affine and less affine insulin-specific binding sites. Bovine insulin contaminated with traces of proinsulin did not induce antibodies specific for the C-chain.Antisera to proinsulin contained equal amounts of high affinity binding sites specific for the C-chain and for the insulin part of the molecule. After absorption of the insulin-specific antibodies these sera can be used for the immunoassay of proinsulin.

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12. [Initial treatment of type I diabetes mellitus with biosynthetic human insulin]

Author

K J, Schlüter, L, Kerp, F, Enzmann, J, Rademacher, M, Lauerbach, W, Bachmann, J, Beyer, J R, Bierich, K, Federlin, F A, Gries, R, Haas, E, Heinze, A, Hübinger, E, Mäser, H, Mehnert, J, Nothjunge, S, Steinhilber, A, Thon, and H G, Velcowsky

Subjects
Adult, Blood Glucose, Male, Time Factors, Diabetes Mellitus, Humans, Insulin, Female, Hemoglobin A, Middle Aged
Published
1983

14. Binding of biosynthetic human insulin to human antibodies and receptors

Author

Klaus J Schlüter, Karl-Georg Petersen, Lothar Kerp, and S. Steinhilber

Subjects
medicine.medical_specialty, Swine, Endocrinology, Diabetes and Metabolism, medicine.medical_treatment, Insulin Antibodies, Antigen-Antibody Complex, Diabetes mellitus, Internal medicine, Insulin receptor substrate, Internal Medicine, Human insulin, medicine, Diabetes Mellitus, Animals, Humans, Insulin, Receptor, Advanced and Specialized Nursing, biology, business.industry, medicine.disease, In vitro, Receptor, Insulin, Insulin receptor, Kinetics, Endocrinology, biology.protein, Antibody, business
Abstract

The binding of biosynthetic human insulin (BHI) and pork insulin to anti-pork insulin antibodies was tested at an insulin concentration of 4 μU/ml. Identical binding data were obtained. The binding of the two insulins to mononuclear lymphocytes was also identical. The data are compared to previous results obtained with synthetic human insulin. Previously, we investigated the in vitro properties of fully synthetic human insulin from Dr. Rittel, Ciba-Geigy, Base.1 Receptor binding of this human insulin was identical to pork insulin. The binding properties of the new BHI from Lilly (Indianapolis) were studied with human antibodies and freshly isolated human monocytes.

Published
1981

15. Starke Herabsetzung von Antigenität und Immunogenität des Rinderinsulins durch Abspaltung der Aminosäuren B1, B2 und B3 unter weitgehender Erhaltung der biologischen Aktivität

Author

K.-G. Petersen, L. Kerp, H. R. Henrichs, R. Geiger, S. Steinhilber, J. Hahn, and H. Kasemir

Abstract

Untersuchungen von Insulinen, die systematischen chemischen Modifikationen unterzogen wurden, sind geeignet, die biologischen und immunologischen Eigenschaften des intakten Insulins bestimmten Teilbereichen der primaren und der raumlichen Struktur des Molekuls topographisch zuzuordnen. Derartige Untersuchungen zielen auf molekulare Strukturwirkungsbeziehungen und liefern gleichzeitig Ansatzpunkte fur planmasige Anderungen einzelner Molekuleigenschaften. Dabei ist vor allem eine Verminderung von unerwunschten immunogenen und antigenen Eigenschaften ohne Beeintrachtigung der Hormonwirkungen des Insulins von Interesse.

Published
1974
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16. Zur Lokalisation von Antikörperbindungsstellen am Insulinmolekül

Author

L. Kerp, H. Kasemir, S. Steinhilber, and F. Kieling

Abstract

Auf Grund vorliegender Immunisierungsversuche von Meerschweinchen mit Rinderinsulin, modifizierten Rinderinsulinmolekulen sowie isolierten sulfonierten A- (SS-A) und B-Ketten (SS-B) des Rinderinsulins wurden fur die untersuchte Tierspecies determinante Gruppen am Rinderinsulinmolekul sowohl verschiedenen Bereichen der A-Kette (Wilson, Dlxon u. Wardlaw [10]; Varandani [8]; Wilson, Aprile u Sasaki [9]) als auch der B-Kette des Rinderinsulinmolekuls (Yagi, Maier U. Pressman [11], Kerp, Kasemir, Kieling u. Keiderling [4]; Wilson, Aprile u. Sasaki [9]) zugeordnet.

Published
1968
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27. Untersuchungen zur Lokalisation der Insertionsstellen Insulinbindender Antikörper am Insulinmolekül

Author

F. Kieling, S. Steinhilber, L. Kerp, and H. Kasemir

Subjects
medicine.medical_specialty, biology, Chemistry, Insulin, medicine.medical_treatment, Heterologous, Preparative ultracentrifugation, Antigen binding, Specific antibody, Endocrinology, Internal medicine, medicine, biology.protein, Homologous chromosome, Antibody, Bovine insulin
Abstract

Summary Using preparative ultracentrifugation it can be demonstrated that in anti-insulin sera from diabetics treated with heterologous insulin, S-sulfonated B chains prepared from ox insulin inhibited the binding of bovine insulin-131 I by specific antibodies, whereas S-sulfonated A chains had no effect. Intact bovine insulin showed the greatest competitive activity. In anti-insulin sera from two sheep and a pig immunized against the homologous sheep and pig insulin the following results were obtained: SS-A chains showed a very small effect, SS-B chains a stronger one and the homologous sheep and pig insulin the strongest displacement of sheep and pig insulin-131 I from antibody binding. In anti-insulin sera from guinea-pigs immunized against ox insulin only SS-B chains and not SS-A chains were able to displace ox insulin-131I from antibody binding to a significant degree. On the other hand, anaphylactic antibodies stimulated by ox insulin and detected by the Schultz-Dale reaction combined with both SS-A chains and SS-B chains.

Published
1969
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31. Besitzt die Proinsulinverunreinigung kommerzieller Insulinpräparate Bedeutung für die Stimulierung von Insulinantikörpern?

Author

S. Steinhilber, L. Kerp, and H. Kasemtr

Subjects
business.industry, Drug Discovery, Molecular Medicine, Medicine, General Medicine, business, Molecular biology, Genetics (clinical)
Abstract

Das untersuchte Antiinsulinserum (Serumpool) von insulinbehandelten Diabetikern enthalt zwei Hauptkomponenten an Antikorperbindungsstellen Ak1 mit hoherer und Ak2 mit geringerer Affinitat zum Rinderinsulinbzw. Rinderproinsulinantigen. Beide Antikorperkomponenten gehen nahzue quantitativ Kreuzreaktionen mit Rinderinsulin bzw. Rinderproinsulin ein.

Published
1970
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32. Induktion einer 'low dose tolerance' gegen Rinderinsulin bei Meerschweinchen

Author

L. Kerp, H. Kasemir, J. Langer, and S. Steinhilber

Subjects
Chemistry, Drug Discovery, Molecular Medicine, General Medicine, Molecular biology, Genetics (clinical)
Abstract

Vier Gruppen von Meerschweinchen erhielten als Vorbehandlung in 3tagigen Abstanden jeweils 8 intravenose Injektionen von 0,002 µg (Gruppe I), 0,02 µg (Gruppe II), 0,2 µg (Gruppe III) bzw. 2,0 µg (Gruppe IV) kristallines Rinderinsulin pro 100 g Korpergewicht in 1,0 ml 0,15 n NaCl. Die Kontrollgruppe erhielt lediglich 1,0 ml 0,15 n NaCl je Versuchstier. Die in den Gruppen I, II und III verabfolgte Insulindosis erwies sich als nicht immunogen. Die hochste Insulindosis in Versuchstiergruppe IV stimulierte eine Antikorperbildung gegen Rinderinsulin. Die intravenose Vorbehandlung mit nicht immunogenen Insulinmengen (Gruppen I–III) bewirkte im Vergleich zur Kontrollgruppe eine signifikante Hemmung der anschliesend durch hohe Rinderinsulindosen s.c. stimulierten Antikorperbildung. Dieses Phanomen wird als Induktion einer „low dose tolerance“ gegen Rinderinsulin interpretiert.

Published
1969
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33. SPECIFIC BINDING OF INSULIN IN THE LIVER OF STEROID-DIABETIC MICE

Author

L. Kerp, K.-G. Petersen, W. Doll, and S. Steinhilber

Subjects
medicine.medical_specialty, biology, business.industry, Endocrinology, Diabetes and Metabolism, medicine.medical_treatment, Insulin, Diabetic mouse, General Medicine, Steroid, Insulin receptor, Endocrinology, Internal medicine, Insulin receptor substrate, medicine, biology.protein, business
Published
1974
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35. An Exercise in Clinical Reasoning: Do You Unpack?

Author

Watkins S, Gaffo AL, Clark AV, and Steinhilber S

Subjects
Adult, Behcet Syndrome complications, Behcet Syndrome drug therapy, Glucocorticoids administration & dosage, Humans, Male, Methylprednisolone administration & dosage, Uveitis drug therapy, Uveitis etiology, Behcet Syndrome diagnostic imaging, Clinical Competence standards, Problem Solving, Uveitis diagnostic imaging
Published
2018
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36. Periorbital edema from apixaban treatment.

Author

Ahmad A and Steinhilber S

Subjects
Aged, Female, Humans, Edema chemically induced, Factor Xa Inhibitors adverse effects, Orbital Diseases chemically induced, Pyrazoles adverse effects, Pyridones adverse effects
Published
2018
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41. A 76-year-old woman with diaphoresis and anxiety.

Author

Steinhilber S, Rodriguez JM, Estrada CA, and Kraemer RR

Subjects
Aged, Diagnosis, Differential, Female, Humans, Hypoglycemia diagnosis, Paraneoplastic Syndromes diagnosis, Pleural Neoplasms complications, Pleural Neoplasms diagnostic imaging, Solitary Fibrous Tumor, Pleural complications, Solitary Fibrous Tumor, Pleural diagnostic imaging, Tomography, X-Ray Computed, Anxiety etiology, Hyperhidrosis etiology, Hypoglycemia complications, Paraneoplastic Syndromes complications
Published
2013
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43. [Initial treatment of type I diabetes mellitus with biosynthetic human insulin].

Author

Schlüter KJ, Kerp L, Enzmann F, Rademacher J, Lauerbach M, Bachmann W, Beyer J, Bierich JR, Federlin K, Gries FA, Haas R, Heinze E, Hübinger A, Mäser E, Mehnert H, Nothjunge J, Steinhilber S, Thon A, and Velcowsky HG

Subjects
Adult, Blood Glucose metabolism, Diabetes Mellitus blood, Female, Hemoglobin A metabolism, Humans, Male, Middle Aged, Time Factors, Diabetes Mellitus drug therapy, Insulin therapeutic use
Published
1983

44. Binding of biosynthetic human insulin to human antibodies and receptors.

Author

Petersen KG, Schlüter K, Steinhilber S, and Kerp L

Subjects
Animals, Diabetes Mellitus immunology, Humans, Insulin biosynthesis, Insulin therapeutic use, Kinetics, Swine, Antigen-Antibody Complex, Insulin metabolism, Insulin Antibodies, Receptor, Insulin metabolism
Abstract

The binding of biosynthetic human insulin (BHI) and pork insulin to anti-pork insulin antibodies was tested at an insulin concentration of 4 microunits/ml. Identical binding data were obtained. The binding of the two insulins to mononuclear lymphocytes was also identical. The data are compared to previous results obtained with synthetic human insulin. Previously, we investigated the in vitro properties of fully synthetic human insulin from Dr. Rittel, Ciba-Geigy, Basel. Receptor binding of this human insulin was identical to pork insulin. The binding properties of the new BHI from Lilly (Indianapolis) were studied with human antibodies and freshly isolated human monocytes.

Published
1981
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48. [Is proinsulin contamination of commercial insulin preparations responsible for the stimulation of insulin antibodies?].

Author

Kerp L, Steinhilber S, and Kasemir H

Subjects
Animals, Antigen-Antibody Complex, Antigen-Antibody Reactions, Antigens analysis, Binding Sites, Cattle, Diabetes Mellitus drug therapy, Diabetes Mellitus immunology, Humans, Insulin blood, Insulin therapeutic use, Iodine Isotopes, Proinsulin blood, Stimulation, Chemical, Antibody Formation drug effects, Drug Contamination, Insulin pharmacology, Insulin Antibodies analysis, Proinsulin pharmacology
Published
1970
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