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Immunogenicity and Bioactivity of Glucagon, Modified at Methionine-27

W J Nooijen, H.J.M. Kempen

Open publisher page 14 citations

Abstract

Porcine glucagon was modified at methionine-27 by methylation or oxidation. Antisera against the glucagon derivatives were obtained. One of these antisera showed a high affinity for glucagon, with no cross-reactivity with gut-GLI 1. Biological activities of these derivatives were assessed on rat hepatocytes. Both derivatives had the same maximal glucose-mobilising activity as native glucagon, but a decrease potency, suggesting a crucial role of methionine in the binding of glucagon to its hepatic receptor.

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What this paper is about

Porcine glucagon was modified at methionine-27 by methylation or oxidation. Antisera against the glucagon derivatives were obtained. One of these antisera showed a high affinity for glucagon, with no cross-reactivity with gut-GLI 1. Biological activities of these derivatives were assessed on rat hepatocytes. Both derivatives had the same maximal glucose-mobilising activity as native glucagon, but a decrease potency, suggesting a crucial role of methionine in the binding of glucagon to its hepatic receptor.

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Available abstract

Porcine glucagon was modified at methionine-27 by methylation or oxidation. Antisera against the glucagon derivatives were obtained. One of these antisera showed a high affinity for glucagon, with no cross-reactivity with gut-GLI 1. Biological activities of these derivatives were assessed on rat hepatocytes. Both derivatives had the same maximal glucose-mobilising activity as native glucagon, but a decrease potency, suggesting a crucial role of methionine in the binding of glucagon to its hepatic receptor.

Key concepts: Glucagon, Methionine, Antiserum, Immunogenicity, Internal medicine, Endocrinology, Methylation, Chemistry

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