An activated S6 kinase in regenerating rat liver.
S6 kinase activity was increased in the regenerating liver 5 h after partial hepatectomy compared with sham-operated liver. The protein kinase activity was eluted from DE-52 column at approximately 250 mM NaCl and was not affected by known regulators of protein kinases. The S6 kinase was further purified by chromatography on peptide R1A13-Sepharose 4B and Sephadex G-150. The molecular weight of the enzyme was estimated to be 4.5 X 10(4) by gel filtration. The enzyme catalyzes the phosphorylation of whole histone, mainly H2B histone, at 75 mM Mg2+. These properties are similar to those of a proteolytically modified Ca2+/phospholipid-independent form of protein kinase C.
D000595:Amino Acid Sequence; D000818:Animals; D002850:Chromatography, Gel; D004789:Enzyme Activation; D006657:Histones / Q000378:metabolism; D008099:Liver / Q000201:enzymology*; D008115:Liver Regeneration; D008274:Magnesium / Q000378:metabolism; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism; D011494:Protein Kinases / Q000378:metabolism*; D051381:Rats; D019893:Ribosomal Protein S6 Kinases; D013379:Substrate Specificity; D013997:Time Factors
D006657:Histones; D011494:Protein Kinases; D019893:Ribosomal Protein S6 Kinases; D011493:Protein Kinase C; D008274:Magnesium