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 journalArticle

17 Citations (Scopus)

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

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Glucagon
Adenylyl Cyclases
Binding Sites
Molecular Weight
Glucagon Receptors
Molecular weight
Enzyme Activation
Enzymes
Electrophoresis
Fluorides
Sodium Dodecyl Sulfate
Polyacrylamide Gel Electrophoresis
Gels
Chemical activation
Hormones
sephadex

ASJC Scopus subject areas

  • Biochemistry

Cite this

Evidence for a dissociable glucagon binding site in a solubilized preparation of myocardial adenylate cyclase. / Klein, I.; Fletcher, M. A.; Levey, G. S.

In: Journal of Biological Chemistry, Vol. 248, No. 15, 01.12.1973, p. 5552-5554.

Research output: Contribution to journalArticle

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