Purification and characterization of protein kinase C from a higher plant, Brassica campestris L.
Protein kinase C (PKC) was partially purified from Brassica campestris L., by successive chromatographies on DEAE-cellulose membrane, hydroxyapatite and phenyl-5PW columns. The purified preparation showed typical characteristics of the conventional type of mammalian PKC that responds to Ca2+, phosphatidylserine, and diacylglycerol or the tumor-promoting phorbol ester, phorbol 12-myristate 13-acetate. The plant PKC activity was apparently associated with a 75-kDa polypeptide that was recognized by an antibody against the catalytic domain of rat PKC. Substrate specificity of the plant PKC was similar to that of the rat PKC. A synthetic peptide corresponding to residues 4-14 of myelin basic protein, which is a selective substrate for the mammalian PKC, was phosphorylated efficiently by the plant PKC. These results indicate the existence of a PKC equivalent in higher plant cells.
Nanmori
T
T
Department of Agricultural Chemistry, Faculty of Agriculture, Kobe University, Japan.
Taguchi
W
W
Kinugasa
M
M
Oji
Y
Y
Sahara
S
S
Fukami
Y
Y
Kikkawa
U
U
D001937:Brassica / Q000201:enzymology*; D002122:Calcium Chloride / Q000494:pharmacology; D002845:Chromatography; D002852:Chromatography, Ion Exchange; D004075:Diglycerides / Q000494:pharmacology; D017886:Durapatite; D015151:Immunoblotting; D007700:Kinetics; D008970:Molecular Weight; D010718:Phosphatidylserines / Q000494:pharmacology; D011493:Protein Kinase C / Q000302:isolation & purification* / Q000378:metabolism*; D013379:Substrate Specificity; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology
D004075:Diglycerides; D010718:Phosphatidylserines; D017886:Durapatite; D011493:Protein Kinase C; D002122:Calcium Chloride; D013755:Tetradecanoylphorbol Acetate; C013965:diolein