Mr. Chandok et Sk. Sopory, IDENTIFICATION OF PHORBOL-MYRISTATE ACETATE STIMULATED KINASE IN ZEA-MAYS, Journal of Plant Biochemistry and Biotechnology, 5(1), 1996, pp. 7-11
Following DEAE-Sephacel and affinity chromatography a highly enriched
lipid stimulated kinase activity could be recovered with a purificatio
n fold of 1725. The peak kinase activity fraction eluted with 0.1 mM c
alcium from phosphatidyl serine affinity chromatography showed a major
protein of 70 kD and a minor band of 55 kD molecular weight and showe
d kinase activity that was stimulated by phorbol myristate acetate in
the presence of phosphatidylserine and calcium. The optimum requiremen
t was 2.5 x 10(-6) M, 1.25 x 10(-4) M, 1 x 10(-4) M, and 1.7 x 10(-6)
M for phorbol myristate acetate, phosphatidyl serine, oleyl acetyl gly
cerol and free calcium respectively. The kinase activity was inhibited
by H-7 and staurosporine. The binding of [H-3]-phorbol myristate acet
ate was associated with purified fraction as resolved by gel electroph
oresis and the kinase activity was also precipitated by animal protein
kinase C antibodies. The present data give strong evidence for the pr
esence of phorbol myristate acetate stimulated kinase in plants.