Abstract
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 R 1A 13-Sepharose 4B and Sephadex G-150. The molecular weight of the enzyme was estimated to be 4.5 × 10 4 by gel filtration. The enzyme catalyzes the phosphorylation of whole histone, mainly H2B histone, at 75 mM Mg 2+. These properties are similar to those of a proteolytically modified Ca 2+/phospholipid-independent form of protein kinase C.
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