[Isolation of protein phosphokinase from a complex form of DNA polymerase alpha from rat liver].
Protein kinase activity was revealed in complex forms of rat liver DNA polymerase alpha containing 3'-5'-exonuclease, primase, helicase, DNA ligase. Protein kinase (mol. mass about 200 kDa) has been partially purified from a specimen of high molecular mass DNA polymerase alpha of nuclear membrane of regenerating liver. The protein kinase activity of the complex form of DNA polymerase alpha was maximal in the cytosol in normal rat liver cells and in the nuclear membrane in dividing cells (40 h after partial hepatectomy). The main phosphokinase properties of this enzyme were determined.
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D000818:Animals; D002467:Cell Nucleus / Q000201:enzymology; D002853:Chromatography, Liquid; D004257:DNA Polymerase II / Q000378:metabolism*; D007425:Intracellular Membranes / Q000201:enzymology; D008099:Liver / Q000201:enzymology* / Q000502:physiology; D008115:Liver Regeneration; D008297:Male; D011494:Protein Kinases / Q000302:isolation & purification* / Q000378:metabolism; D051381:Rats
D011494:Protein Kinases; D004257:DNA Polymerase II
Vydelenie proteinfosfokinazy iz kompleksnoĭ formy DNK-polimerazy alpha pecheni krysy.