Phospholipid-dependent and EGTA-inhibited protein kinase from maize seedlings.

Chromatography of a maize seedling extract on DEAE-cellulose, followed by Octyl-Sepharose yielded a fraction with protein kinase activity which was stimulated by phosphatidylserine plus diolein. The activity was not enhanced by calcium ions but was inhibited by chelating agents and could then be restored by the addition of calcium ions. All these facts indicated that the maize protein kinase was similar to mammalian protein kinase C. The maize enzyme phosphorylated myelin basic protein (MBP) and histone H1, but the MBP-peptide4-14 and protamine were poor substrates for the enzyme. Further purification of the enzyme fraction followed by phosphorylation and SDS-polyacrylamide gel electrophoresis, revealed two labeled bands of Mw 59 and 83 kDa the former of which probably being the protein kinase C.