USE OF A COMPETITIVE PROTEIN-BINDING ASSAY FOR ADENOSINE 3′:5′-PHOSPHATE FOR THE STUDY OF BOVINE CORPUS LUTEUM ADENYLATE CYCLASE
- 1 April 1977
- journal article
- research article
- Published by Bioscientifica in Journal of Endocrinology
- Vol. 73 (1) , 123-134
- https://doi.org/10.1677/joe.0.0730123
Abstract
SUMMARY: The use of a competitive protein-binding assay for cyclic AMP, utilizing the binding protein purified from bovine adrenal cortex, for the study of adenylate cyclase activity of the washed 600 g sediment of bovine corpus luteum is validated. A specific assay for cyclic AMP could only be achieved by removal of the degradation products of ATP on a precipitate of nascent BaSO4. Simple dilution of the sample before assay was not sufficient to eliminate interference from degradation products of ATP. An observed variability in optimal ATP substrate and tissue concentrations is thought to reflect variability in the enzymic profile of the cyclic corpus luteum. Optima with respect to F−, Mg2+ and pH are more clearly defined and are similar to those reported for adenylate cyclase systems of other tissues.Keywords
This publication has 2 references indexed in Scilit:
- Dissociation and reassociation of the phosphorylated and nonphosphorylated forms of adenosine 3':5' -monophosphate-dependent protein kinase from bovine cardiac muscle.Journal of Biological Chemistry, 1976
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951