title: A hepatic soluble cyclic nucleotide-independent protein kinase. Stimulation by basic polypeptides.
abstract: Enzymatic phosphorylation of cytoplasmic proteins by a cyclic nucleotide-independent protein kinase (casein kinase of a classical type) in rat liver is stimulated greatly, sometimes more than 10-fold, by polycations, particularly by basic polypeptides such as polylysine, histone, and protamine. These basic polypeptides themselves do not serve as phosphate acceptors but act as stimulators for the reaction by interacting with cytoplasmic proteins rather than with enzyme. The stimulatory effect varies with substrates employed; with casein and phosvitin the stimulation does not exceed 2- to 3-fold. The cytoplasmic endogenous phosphate acceptor proteins measurable in the presence of basic polypeptides are abundant for this species of protein kinase.
mesh_terms: D000818:Animals; D004789:Enzyme Activation; D006657:Histones / Q000494:pharmacology; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D009712:Nucleotides, Cyclic / Q000494:pharmacology; D010455:Peptides / Q000494:pharmacology*; D011107:Polylysine / Q000494:pharmacology; D011494:Protein Kinases / Q000378:metabolism*; D051381:Rats
chemical_list: D006657:Histones; D009712:Nucleotides, Cyclic; D010455:Peptides; D011107:Polylysine; D011494:Protein Kinases