[Catalytic properties of soluble 3':5'-AMP-dependent protein kinase of rabbit myocardium].
The results of kinetic studies are presented for two forms of soluble 3':5'-AMP-dependent protein kinase, obtained by DEAE-cellulose and hydroxyl apatite chromography. The pH optimum for both forms of the enzyme is shown to be 6.8-7.0; their activity is the highest at ionic strength of 0.023. Both forms of the enzyme at the above values of pH and ionic strength are thermoinactivated by the exponential law, their inactivation rate constants rise with temperature. Calcium ions in a concentration of 1.10(6)-2.10(-3) M have no effect on their activity.
D000818:Animals; D002118:Calcium / Q000494:pharmacology; D000242:Cyclic AMP / Q000494:pharmacology*; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism; D007700:Kinetics; D009206:Myocardium / Q000201:enzymology*; D009994:Osmolar Concentration; D011494:Protein Kinases / Q000302:isolation & purification / Q000378:metabolism*; D011817:Rabbits
D007527:Isoenzymes; D000242:Cyclic AMP; D011494:Protein Kinases; D002118:Calcium
Kataliticheskie svoĭstva rastvorimoĭ 3':5'-AMP-zavisimoĭ proteinkinazy miokarda krolikov.