title: Fractionation and partial purification of rat liver nuclear protein kinases.
abstract: We have fractional and partially purified several rat liver nuclear protein kinases by utilizing endogenous (nonhistone proteins) and exogenous acidic (dephosphophosvitin) and basic (lysine-rich histone) protein substrates. Three enzymes were active towards endogenous substrates, two towards dephosphophosvitin and two towards lysine-rich histone. Of the latter only one was cAMP-dependent, however, only minimal cAMP binding activity was detected. Several features of these enzyme reactions are described revealing distinct differences in the characteristics of each of these enzymes.
mesh_terms: D000818:Animals; D002467:Cell Nucleus / Q000201:enzymology; D002868:Chromosomal Proteins, Non-Histone / Q000378:metabolism; D000242:Cyclic AMP / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008297:Male; D010774:Phosvitin / Q000031:analogs & derivatives / Q000378:metabolism; D006656:Protamine Kinase / Q000378:metabolism; D011494:Protein Kinases / Q000302:isolation & purification* / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains
chemical_list: D002868:Chromosomal Proteins, Non-Histone; C018898:dephosphophosvitin; D010774:Phosvitin; D000242:Cyclic AMP; D011494:Protein Kinases; C026813:protein kinase NII; D006656:Protamine Kinase