Protein kinase in cultured plant cells.
A protein kinase (EC 2.7.1.37) which phosphorylates histones was purified partially from the soluble fractions of cultured plant cells. The optimum pH was 7.5 to 9.0. The activity wasnot stimulated by exogeneous cyclic AMP. It was thermolabile and completely dependent on the presence of Mg2+ or Mn2+ for activity. p-Chloromercuribenzoate inactivated this enzyme and this inactivation was overcome by mercaptoethanol.
D000242:Cyclic AMP / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D008274:Magnesium / Q000494:pharmacology; D008345:Manganese / Q000494:pharmacology; D010944:Plants / Q000201:enzymology*; D006656:Protamine Kinase / Q000302:isolation & purification / Q000378:metabolism*; D011494:Protein Kinases / Q000378:metabolism*; D013439:Sulfhydryl Reagents / Q000494:pharmacology; D013696:Temperature
D013439:Sulfhydryl Reagents; D008345:Manganese; D000242:Cyclic AMP; D011494:Protein Kinases; D006656:Protamine Kinase; D008274:Magnesium