Comparative Study of Three Male Genital Acid Phosphatases.

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Abstract
Despite their origin from non-homologous glands, acid phosphatases from human seminal plasma, rat preputial gland, and guinea pig seminal vesicle show similar pH optima and Michaelis constants, and are similarly fluoride-, tungstate-, molybdate-, oxalate-, L- tartrate-, and ethanol-sensitive and formaldehyde-resistant. The pH optima were raised by 0.5-1.0 pH unit with a 10-fold increase in substrate concn. (phenolphthalein phosphate). The 3 enzymes are activated by serum albumin, that of the preputial gland less than the other 2.

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