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A human platelet cytosolic phosphoinositide-specific phospholipase C, one of four PLC activity peaks separated by column chromatographies, designated as cPLC-I, was purified to homogeneity. The cPLC-I exhibited an apparent Mr of 145 kDa by SDS-polyacrylamide gel electrophoresis and was immunologically identified to be PLC-gamma 2. It hydrolyzed PI and PIP2 at optimum pH of 5.5-6.0. Deoxycholate and cholate inhibited the enzyme activity to hydrolyze two substrates. Calcium was required to obtain the maximal activity for PI- and PIP2-hydrolysis at concentration of 10(-3) M and 10(-5) M, respectively. Hg2+ (1 microM) inhibited strongly the enzyme activity.
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