[Multiple forms of protein kinase from the cytoplasm of Ehrlich ascites carcinoma cells].
The composition of protein kinases and cAMP-binding proteins of the soluble fraction of Ehrlich ascite carcinoma cell cytoplasm was studied. Using ion-exchange chromatography on DEAE-cellulose, two forms of the histone kinase activity were found in the cytosol. One of them corresponded to the catalytic subunit of cAMP-dependent protein kinases, the other one--to protein kinase II. Chromatographic and kinetic analyses revealed the presence of two cAMP-binding proteins with Kd values for cAMP equal to 2 and 8 nM. One of these proteins was identified as protein kinase II, while the other one was devoid of the protein kinase activity and the ability to dissociate during cAMP binding. The existence of a high and low molecular weight forms of casein kinase (Mr = 180 000 and 32 000, respectively) in Ehrlich ascite carcinoma cell cytosol was demonstrated.
D000818:Animals; D002286:Carcinoma, Ehrlich Tumor / Q000201:enzymology*; D002352:Carrier Proteins / Q000302:isolation & purification*; D002373:Cyclic AMP Receptor Protein; D007527:Isoenzymes / Q000302:isolation & purification* / Q000378:metabolism; D007700:Kinetics; D051379:Mice; D011494:Protein Kinases / Q000302:isolation & purification* / Q000378:metabolism; D011953:Receptors, Cyclic AMP / Q000302:isolation & purification*
D002352:Carrier Proteins; D002373:Cyclic AMP Receptor Protein; D007527:Isoenzymes; D011953:Receptors, Cyclic AMP; D011494:Protein Kinases
Mnozhestvennye formy proteinkinaz iz tsitoplazmy kletok astsitnoĭ kartsinomy Erlikha.