1979 年 99 巻 1 号 p. 83-89
Monospecific antiserum to purified human prostatic acid phosphatase was produced in rabbits. Prostatic acid phosphatase treated with neuraminidase retained all enzyme activity before treatment and reacted with the antiserum. The enzyme treated with urea, sodium dodecyl sulfate, 2-mercaptoethanol and guanidine hydrochloride lost all enzyme activity and did not react with the antiserum. We demonstrated that the antibody to the prostatic acid phosphatase can protect the enzyme specifically against heat and pH inactivation. When the prostatic acid phosphatase was coupled with the antibody, enzyme activity was markedly stabilized at pH 4.6-5.8 at 56°. Prostatic acid phosphatase activities in human sera were assayed using the antibody. The activity values were high in sera of patients with prostatic carcinoma and low in sera of patients with prostatic hypertrophy and normal subjects.