Two isozymes of PKC found in HL-60 cells show a difference in activation by the phorbol ester TPA.
Cytosol from untreated cells and a detergent extract of the particulate fraction from TPA-treated HL-60 cells were analyzed for protein kinase C activity by consecutive column chromatography on Mono Q and hydroxyapatite. From both preparations two separate peaks of enzyme activity were obtained. The first peak, eluting at lower salt concentrations, is activated at lower TPA concentrations (3 X 10(-9) M) than the other (10(-7) M), which was eluted at higher salt concentrations.
Beh
I
I
Institute of Biochemistry, German Cancer Research Center, Heidelberg.
Schmidt
R
R
Hecker
E
E
D000818:Animals; D002460:Cell Line; D002853:Chromatography, Liquid; D004305:Dose-Response Relationship, Drug; D004789:Enzyme Activation; D007527:Isoenzymes / Q000378:metabolism*; D051379:Mice; D011493:Protein Kinase C / Q000378:metabolism*; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology*
D007527:Isoenzymes; D011493:Protein Kinase C; D013755:Tetradecanoylphorbol Acetate