Phosphatase-Antiphosphatase Reaction

Abstract

Summary Inhibition of the α-glycerophosphatase activity of intact dried yeast by specific antiserum produced in the rabbit indicates that the enzyme is located on the surface of the cells. Although easily extracted with water, its activity was manifested as an integral cellular component. Live yeast was phosphatase-inactive until air-dried but capable of inciting the production of antiphosphatase antibody in the rabbit. Antiserum against the partially purified yeast α-glycerophosphatase inhibits the hydrolysis of α-glycerophosphate by the enzyme. The degree of inhibition is dependent upon the concentration of substrate and antiserum, respectively. The data show that the specific substrate, α-glycerophosphate, competes with antiphosphatase antibody for the specific active combining sites in the enzymes. The theoretical implications of these findings are discussed.