title: [Purification and properties of two forms of soluble 3',5'-AMP-dependent protein kinase from rabbit myocardium].
abstract: Two forms of 3' : 5'-AMP-dependent protein kinase were purified from the rabbit myocardium. The concentrations of 3' : 5'-AMP-necessary for maximum stimulation of form I and II were the same but the second form of the enzyme was activated by this concentration to a greater extent. The seeming Km by ATP for the both forms in the presence of 3' : 5'-AMP is found to be 8.3.10(-6)M. For enzyme form I the seeming Km by histone H1 was 0.43 mg/ml and for form II--0.67 mg/ml.
mesh_terms: D000818:Animals; D000242:Cyclic AMP / Q000494:pharmacology*; D004789:Enzyme Activation; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism; D007700:Kinetics; D009206:Myocardium / Q000201:enzymology*; D011494:Protein Kinases / Q000302:isolation & purification / Q000378:metabolism*; D011817:Rabbits
chemical_list: D007527:Isoenzymes; D000242:Cyclic AMP; D011494:Protein Kinases
vernacular_title: Ochistka i svoĭstva dvukh form rastvorimoĭ 3':5'-AMP-zavisimoĭ proteinkinazy iz miokarda krolikov.