Quantitative Ergebnisse zur Lokalisation determinanter Gruppen am Insulinmolek�l

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

doi:10.1007/bf00592984

Cited by 4 publications

(2 citation statements)

References 9 publications

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“…These changes in affinity can be measured separately for each of the main components of insulin binding IgG-antibodies Aki and Ak2, occurring simultaneously in all species investigated, also being directed against different regions of the insulin molecule 14 and different in clinical effects. 12 Comparison of the binding of bovine insulin and modified insulins by the antibody component Aki with high affinity reveals that Phe B l contributes 2.6 kcal/Mols i.e.…”

Section: Immunologic Activitiesmentioning

confidence: 99%

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

Kerp¹,

Steinhilber²,

Kasemir³

et al. 1974

Diabetes

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The influence of splitting off the N-terminal amino acids Bl, 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 -AF°i for complex formation between high affinity antibodies Aki and des-Phe Bl -insulin or des-(Phe-Val) Bl " 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) Bl " 3 -[Pyr B4 ] insulin.The standard free energy -AF°2 for complex formation between low affinity antibodies Ak2 and des-Phe Bl -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-Phe Bl -insulin and des-(PheVaI) Bl " 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) Bl " 3 -[Pyr B4 ] 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-Phe Bl -insulin, to 86±3 per cent for des-(Phe-Val) Bl " 2 -insulin and to 68±6 per cent for des-(Phe-Val-Asn) Bl " 3 -[Pyr B4 ] insulin. DIABETES 23:651-56, August, 1974.Lindsay and Shall 16 studied the immunologic and biologic properties of bovine insulin modified by acetylation. Substitution of the N-terminal amino acid of the B-chain phenylalanine (Phe Bl ) by acetyl-, acetoacetyl-and thiazolidine groups led to a large decrease in the immunoreactivity of bovine insulin for insulin antibodies raised in guinea pigs, whereas these substitutions did not affect biologic activities.From the Medical University Clinic, Freiburg i. Br., and Farbwerke Hoechst AG, vorm. Meister Lucius und Bruning, Frankfurt (M)-Hoechst, Germany.

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Section: Immunologic Activitiesmentioning

confidence: 99%

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

Kerp¹,

Steinhilber²,

Kasemir³

et al. 1974

Diabetes

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show abstract

“…The toxicity of either substance was very low. The biological effects, measured for instance on histamine weals in human subjects after oral application of 3 mg of Dimethpyrindene and 1.5 mg of HS 592, are of about the same order of magnitude (6). Inhibition is at a maximum after intervals of about three to four hours; the effect of both substances is seen to decline after an interval of ten hours.…”

Section: Fig I the Chemical Configuration Of Dimethpyrindene And Amentioning

confidence: 85%

Dimethpyrindene and a New Antihistamine Hs 592 (Sandoz) in the Treatment of Severe Chronic Urticaria

Søbye¹,

Ulrich²

1968

Allergy

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Die Immunologie des Insulins

Kerp¹,

Henrichs²,

Kasemir³

1975

Diabetes Mellitus · A

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Quantitative Ergebnisse zur Lokalisation determinanter Gruppen am Insulinmolek�l

Cited by 4 publications

References 9 publications

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

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

Dimethpyrindene and a New Antihistamine Hs 592 (Sandoz) in the Treatment of Severe Chronic Urticaria

Die Immunologie des Insulins

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