[Several properties of 3':5'-AMP-dependent skeletal muscle protein kinases in normal rats and following physical exertion to fatigue].
Three fractions of rat adenosine-3',5'-monophosphate-dependent protein kinase were isolated, partially purified in buffer concentration gradient at normal state and after long-term physical loading and studied. It is found that first two fractions of protein kinases at normal state and after intensive muscular work have similar activities with and without cAMP, apparent Km values for ATP and total histone and half-maximal stimulation by cyclic AMP, but they differed from the third fraction. There are differences in some kinetic parameters and in the cyclic AMP stimulated activities between protein kinases after physical loading. The data obtained suggest the existence of at least two kinases in rat skeletal muscle. The isoenzymes differ in their activities during fatigue.
D000818:Animals; D000242:Cyclic AMP; D004789:Enzyme Activation; D005221:Fatigue / Q000201:enzymology*; D007527:Isoenzymes / Q000378:metabolism*; D008297:Male; D009132:Muscles / Q000201:enzymology*; D010766:Phosphorylation; D006656:Protamine Kinase / Q000378:metabolism; D011494:Protein Kinases / Q000378:metabolism*; D051381:Rats
D007527:Isoenzymes; D000242:Cyclic AMP; D011494:Protein Kinases; D006656:Protamine Kinase
Nekotorye svoĭstva 3':5'-AMP-zavisimykh proteinkinaz skeletnykh myshts krys v norme i pri fizicheskoĭ nagruzke do utomleniia.