Immunogenicity and bioactivity of glucagon, modified at methionine-27.
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.
D000273:Adipose Tissue / Q000187:drug effects / Q000378:metabolism; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001681:Biological Assay; D005934:Glucagon / Q000031:analogs & derivatives* / Q000276:immunology / Q000494:pharmacology; D005947:Glucose / Q000378:metabolism; D007700:Kinetics; D008745:Methylation; D010084:Oxidation-Reduction; D051381:Rats; D011956:Receptors, Cell Surface / Q000378:metabolism; D013552:Swine
D000596:Amino Acids; D011956:Receptors, Cell Surface; D005934:Glucagon; D005947:Glucose