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Identification of a cAMP-dependent protein kinase in bovine and human follicular fluids
L S Yang1, A L Kadam, S S Koide
1Center for Biomedical Research, Population Council, New York, NY 10021.
Biochemistry and Molecular Biology International
|November 1, 1993
Abstract:
A soluble protein kinase (PK) was purified from bovine and human follicular fluids (FF) by ultrafiltration through a PM-10 membrane followed by chromatography on heparin-agarose, DEAE-cellulose and cellulose phosphate columns. The PK phosphorylated calf thymus histones and endogenous FF proteins having estimated Mrs of 40, 62, 128 and 180 KD. cAMP enhanced PK activity; whereas protein kinase A (PKA)-inhibitor peptide blocked the activity. The present findings suggest that the enzyme is a cAMP-dependent PK.