Immunochemical investigation of human seminal plasma acid phosphatase.

Acid phosphatase of human seminal plasma is inhibited in presence of normal rabbit serum involving non-competitive mechanism whereas this character is normalized and activity is stabilized in presence of its rabbit antiserum. Kinetic studies on stabilization of acid phosphatase by antiserum were combined by L-tartrate, a specific inhibitor of prostatic acid phosphatase. L-tartrate, a specific inhibitor of prostatic acid phosphatase. L-tartrate inhibited the enzyme in presence and absence of normal and antiserum by competitive mechanism and percentage of inhibition of L-tartrate was involve in the binding with acid phosphatase antibodies. The kinetics of heat denaturation of acid phosphatase suggested that seminal acid phosphatase is more heat labile in presence and absence of normal serum than in presence of antiserum. The temperature of denaturation corresponding to half the initial activity(T 1/2) in presence of normal and antisera were 34 degrees and 66 degrees C respectively. NOn-linearity of Arrhenius plots for denaturation rates of the enzyme suggested various conformational states for denaturation yielding Ea varying between 20.08 and 5.03 Kcals at 25-65 degrees C.