A reassessment of structure-function relationships in glucagon. Glucagon1-21 is a full agonist

D. E. Wright, V. J. Hruby, M. Rodbell

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Abstract

Glucagon1-21 has been prepared by treating native glucagon with carboxypeptidase A. Purified glucagon1-21 did not contain detectable methionine (<0.001 residue/mol) and the activity of the compound did not change after treatment with cyanogen bromide as has been shown with native glucagon. Glucagon1-21 stimulates hepatic adenylate cyclase activity to the same extent as native glucagon but with 0.1% the potency. Glucagon1-21 also displayed 0.1% the binding affinity of native glucagon to the glucagon receptor in hepatic membranes. Glucagon22-29 alone or in combination with glucagon1-21 did not activate adenylate cyclase or displace 125I-glucagon from its receptor. The finding that glucagon1-21 is a full agonist on adenylate cyclase is discussed in relation to the structure-function relationships required for the biological action of glucagon.

Original languageEnglish (US)
Pages (from-to)6338-6340
Number of pages3
JournalJournal of Biological Chemistry
Volume253
Issue number18
StatePublished - Dec 1 1978

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ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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