Species-dependent isoenzyme subtypes of membrane-bound cyclic AMP-dependent protein kinase in highly purified cardiac sarcolemma.
Highly purified sarcolemma from dog and pig cardiac muscle has been shown to contain significant activities of a membrane-bound cyclic AMP-dependent protein kinase. In addition, these membranes undergo endogenous phosphorylation when incubated with Mg2+ and [gamma-32P]ATP. By comparing 32P-labelled patterns obtained with [gamma-32P]ATP and the photoaffinity label 8-azidoadenosine 3':5'-[32P]monophosphate (8-azido-cyclic [32P]AMP), we have demonstrated that, whereas the major kinase isoenzyme in dog sarcolemma was Type II, that in the pig membrane was the Type I isoenzyme.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000345:Affinity Labels / Q000378:metabolism; D000818:Animals; D001386:Azides / Q000378:metabolism; D000242:Cyclic AMP / Q000031:analogs & derivatives / Q000378:metabolism; D004285:Dogs; D004591:Electrophoresis, Polyacrylamide Gel; D007527:Isoenzymes / Q000378:metabolism*; D009206:Myocardium / Q000201:enzymology*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D012508:Sarcolemma / Q000201:enzymology; D013045:Species Specificity; D013552:Swine
D000345:Affinity Labels; D001386:Azides; D007527:Isoenzymes; C017042:8-azidoadenosine-3',5'-monophosphate; D000255:Adenosine Triphosphate; D000242:Cyclic AMP; D011494:Protein Kinases