THE WHEAT LEAF PHOSPHATASES: V. SOME PROPERTIES OF THE ENZYME SYSTEM HYDROLYZING β-GLYCEROPHOSPHATE IN CRUDE JUICE PREPARATIONS

Abstract

Wheat leaf press juice contains an enzyme that has β-glycerophosphatase activity, which has a pH optimum close to pH 5.7. The enzyme is inhibited by orthophosphate, pyrophosphate, and 10−4 M fluoride. Fluoride inhibition can be abolished by thorough dialysis. Fluoride partially protects the enzyme from denaturation by heat.Enzyme kinetics shows that the log of the enzyme concentration is proportional to the log of the rate of liberation of orthophosphate from the substrate in the presence of excess substrate (0.2 M to 0.6 M) at pH 5.7. This observation can be used for quantitation of the enzyme.