Studies on human prostatic acid phosphatase. IV. Stabilization of prostatic acid phosphatase against thermal inactivation by the homologous antibody.

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Abstract
Antibody against purified human prostatic acid phosphatase (orthophosphoric monoester phosphohydrolase, EC 3.1.3.2, a serum diagnostic marker for prostatic cancer) was produced in rabbits. The antiserum stabilized the activity of the enzyme against heat treatment, such as incubation at 56.degree. C for 30 min, whereas normal rabbit serum displayed no stabilizing effect. IgG was isolated by ammonium sulfate fractionation and affinity chromatography on a Protein A-Sepharose CL-4B column. The IgG fraction showed a remarkable heat-stabilizing effect on prostatic acid phosphatase (PAPase) and the heat-stabilizing factor was purified 4.2-fold by the IgG isolation method. A complex of PAPase and PAPase specific IgG was separated from a mixture of PAPase and antiserum by a combination of Protein A-Sepharose CL-4B column and Sephacryl S-300 column chromatographies. The immune complex displayed heat stability. IgG which failed to bind PAPase had no heat-stabilizing effect on PAPase. Fab fragments obtained by papain digestion showed a low heat-stabilizing effect whereas F(ab'')2 fragments obtained by pepsin digestion displayed a heat-stabilizing effect comparable with that of the IgG fraction.

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