Rabbit skeletal muscle protein kinase. Conversion from cAMP dependent to independent form by chemical perturbations.
Protein kinase isolated from rabbit skeletal muscle can be reversibly converted from the cAMP dependent form to the indepent form by chaotropic salts and urea. A similar but irreversible conversion can also be induced by trypsin digestion of the holoenzyme. The dissociation of cAMP dependent protein kinase by low concentrations of thiocyanate raises the possibility of isolating both native regulatory and catalytic subunits. From various changes in enzymatic activity caused by urea and trypsin perturbation, it is proposed that the conversion of protein kinase from the cAMP dependent to the independent form is due primarily to preferential modification of the regulatory subunit of the holoenzyme.
D000818:Animals; D000242:Cyclic AMP / Q000494:pharmacology*; D004789:Enzyme Activation / Q000187:drug effects; D046911:Macromolecular Substances; D008970:Molecular Weight; D009132:Muscles / Q000187:drug effects / Q000201:enzymology*; D011494:Protein Kinases / Q000302:isolation & purification / Q000378:metabolism*; D011817:Rabbits; D013861:Thiocyanates / Q000494:pharmacology; D014357:Trypsin; D014508:Urea
D046911:Macromolecular Substances; D013861:Thiocyanates; D014508:Urea; D000242:Cyclic AMP; D011494:Protein Kinases; D014357:Trypsin