Partial characterization of protein kinase C and inhibitor activity of protein kinase C in rabbit peritoneal neutrophils.
Analysis of the cytosol fraction containing protein kinase C activity from rabbit peritoneal neutrophils by DEAE-cellulose chromatography identified protein kinase C activity in the fractions eluted with 0.08 M-0.14 M NaCl and protein kinase C inhibitor activity in the fraction eluted with 0.16 M-0.5 M NaCl. On further analysis by Sephadex G-150 gel filtration, one peak of protein kinase C and two peaks of inhibitor activity were identified. The peak of protein kinase C and two peaks of inhibitor activity were identified. The peak of protein kinase C activity eluted at Ve/Vo 1.6 corresponding to a Stokes radius of 35 A. The first peak of the inhibitor activity eluted at Ve/Vo 1.4 and the second peak of the inhibitor activity eluted at Ve/Vo 2.5. The peak of phosphoprotein phosphatase activity does not coincide with the peaks of inhibitor activity of protein kinase C.
Huang
C K
CK
Oshana
S C
SC
D000818:Animals; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D003600:Cytosol / Q000201:enzymology; D009504:Neutrophils / Q000201:enzymology*; D010718:Phosphatidylserines / Q000494:pharmacology; D011493:Protein Kinase C / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D011817:Rabbits; D012685:Sepharose / Q000031:analogs & derivatives; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology
D010718:Phosphatidylserines; C020927:phenyl-sepharose; D012685:Sepharose; D011493:Protein Kinase C; D013755:Tetradecanoylphorbol Acetate