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 language||English (US)|
|Number of pages||3|
|Journal||Journal of Biological Chemistry|
|State||Published - 1973|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology