Identification of a cAMP-dependent protein kinase in bovine and human follicular fluids.
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.
Yang
L S
LS
Center for Biomedical Research, Population Council, New York, NY 10021.
Kadam
A L
AL
Koide
S S
SS
D000818:Animals; D001826:Body Fluids / Q000201:enzymology; D002417:Cattle; D002848:Chromatography, DEAE-Cellulose; D017868:Cyclic AMP-Dependent Protein Kinases / Q000302:isolation & purification* / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006657:Histones / Q000378:metabolism; D006801:Humans; D006080:Ovarian Follicle / Q000201:enzymology*; D010766:Phosphorylation
D006657:Histones; D017868:Cyclic AMP-Dependent Protein Kinases