Properties of the acid phosphatases of erythrocytes and of the human prostate gland

Abstract

The prostatic and red-cell acid phosphatases were studied with respect to pH-hydrolysis curves of phenyl phosphate, the relative rates of hydrolysis of alpha- and beta-glycero-phosphates, and the effect of Mg. The presence of 2 acid phosphatases in the red cells was confirmed. No evidence for enzyme activation by Ca, Cr, Co, Cu, Fe, Mn, Ni or Zn was obtained. Cu completely destroyed the red-cell enzyme; while Fe, in acetate buffer, strongly inhibited the prostatic enzyme, but had no such action in citrate buffer. Glycine and alanine had no effect on either prostatic or red-cell phosphatases. Cysteine slightly activated both enzymes. The effects of ethanol, acetone, formaldehyde and certain organic acid radicals on acid phosphatase activity were studied. L-Tartrate, while not affecting the acid phosphatases of plasma and red cells, inhibited other acid phosphatases particularly that of the prostate, and the nature of this action was studied and discussed. Stilbestrol had no direct effect on any of the acid phosphatases.