The cytosolic fraction of soybean sprouts contains three PI-specific PLC enzymes (F-I, F-II, and F-III), which can be separated by Matrex green gel chromatography. Their catalytic properties are different from each other in their requirements for $Ca^{2+}$ and sodium deoxycholate. The expression of these enzymes under various conditions are growth-stage specific and tissue specific. The F-Il fraction was especially active during the early growth stage. However, the activities of the F-I and F-III fractions gradually increased from the early to late growth stages. The specific activity of individual PLC enzymes in soybean sprout tissue did not show the same pattern. Among the various soybean sprout tissues, higher PLC activity appeared in the actively elongating hypocotyl tissue. Light, 2,4-D, and BA slightly induced the activities of all three PLC enzymes. On nondenaturing polyacrylamide gels, the PI hydrolyzing activities of F-I and F-I1 appeared as a single peak, while the F-III activity was divided into two separate peaks. Since the molecular weight of the upper PLC activity peak of F-III was nearly twice that of the lower peak, F-III PLC may exist as a mixture of monomer and dimeric enzymes.