Evidence for a dissociable glucagon binding site in a solubilized preparation of myocardial adenylate cyclase

I. Klein, M. A. Fletcher, G. S. Levey

Research output: Contribution to journalArticlepeer-review

17 Scopus citations

Abstract

A solubilized preparation of myocardial adenylate cyclase was chromatographed on Sephadex G 100. Binding of 125I glucagon and fluoride stimulatable adenylate cyclase activity occurred in the elution fractions excluded from the gel suggesting a molecular weight greater than 100,000 for the enzyme receptor site complex. Prior incubation of the binding peak with glucagon shifted its elution pattern on Sephadex G 100 to a smaller molecular weight peak of approximately 20,000 as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The findings are consistent with a dissociable receptor site for glucagon on myocardial adenylate cyclase and may provide a mechanism for activation inactivation of the enzyme following hormone binding.

Original languageEnglish (US)
Pages (from-to)5552-5554
Number of pages3
JournalJournal of Biological Chemistry
Volume248
Issue number15
StatePublished - Dec 1 1973

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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