Glucagon1-6 binds to the glucagon receptor and activates hepatic adenylate cyclase.
J Biol Chem, 1979/1/25;254(2):268-9.
PMID: 216670
Abstract
A fragment of glucagon encompassing its first six NH2-terminal residues (His-Ser-Gln-Gly-Thr-Phe) binds to the glucagon receptor and stimulates adenylate cyclase activity in rat liver plasma membranes. Glucagon1-6 is a partial agonist since it stimulates, at saturating concentrations, to the extent of 75% of the maximal activity given by the native hormone. The binding affinity and potency of glucagon1-6 are 0.001% the native hormone. Discussed are the implications of these findings on the structure-function relationships required for the action of glucagon and for preparing clinically useful analogs of the hormone.
MeSH terms
Adenylyl Cyclases; Animals; Enzyme Activation; Glucagon; Kinetics; Liver; Oligopeptides; Rats; Receptors, Cell Surface
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