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Title: Identification of a cAMP-dependent protein kinase in bovine and human follicular fluids. Author: Yang LS, Kadam AL, Koide SS. Journal: Biochem Mol Biol Int; 1993 Nov; 31(3):521-5. PubMed ID: 8118427. 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.[Abstract] [Full Text] [Related] [New Search]