Purification of a protein inhibitor of adenosine 3':5'-monophosphate-dependent protein kinase from bovine myocardium by a non-denaturing procedure.
The activities of adenosine 3':5'-monophosphate (cyclic AMP)-dependent protein kinase may be partially controlled by a ubiquitous acidic heat-stable protein which inhibits the phosphotransferase reaction by interaction with the catalytic subunit of protein kinase (Walsh, D.A. et al. (1971), J. Biol. Chem. 246, 1977-1985). Since reported purification of this inhibitor involved subjecting tissue extracts to denaturing conditions, its existence under physiological conditions remained uncertain. A protein inhibitor, molecular weight 22,500, has been isolated from bovine myocardium by methods that do not include exposure to extreme heat or acid precipitation. The activity of this acidic protein is destroyed by exposure to trypsin and is unaffected by treatment with neuraminidase, RNAse or DNAse.
D000818:Animals; D002417:Cattle; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D000242:Cyclic AMP / Q000378:metabolism; D004791:Enzyme Inhibitors / Q000302:isolation & purification*; D008970:Molecular Weight; D009206:Myocardium / Q000201:enzymology*; D011489:Protein Denaturation; D047428:Protein Kinase Inhibitors; D014357:Trypsin
D004791:Enzyme Inhibitors; D047428:Protein Kinase Inhibitors; D000242:Cyclic AMP; D014357:Trypsin