Protein kinase C (PKC) from mycelium (Basidiomycotina) was purified by affinity chromatography using activated agarose (Affigel 15) coupled with the protein kinase inhibitor -(2-aminoethyl)-5-isoquinolinesulphonamide hydrochloride. Using buffer containing 2.0 M-arginine. PKC activity eluted as a single peak corresponding to a protein with apparent molecular mass of approximately 68000 Da as estimated by SDS-PAGE. The enzyme was not stimulated by Ca alone, and activation by phosphatidylserine (PS) was significant only at 10 M-Ca. However, the activity was enhanced by the addition of 1,2-dioctanoyl--glycerol in the presence of PS and Ca. Additionally, although sensitivity was lower than for mammalian PKC, the enzyme was activated by a tumour-promoting phorbol ester, phorbol-12-myristate 13-acetate (PMA). The saturation concentration of PMA was 50 μg ml, which was 5 × 10 times the value for mammalian PKC.


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