Cytochemistry and biochemistry of acid phosphatases. I. Cytochemistry and isoelectric focussing of acid phosphatases of the rat ventral prostate.

Acid phosphatases of the rat ventral prostate were studied cytochemically using different substrates. The results were compared to findings on isoelectric focussing gels stained for acid phosphatase activity. This is a highly specific and reproducible method which allows the distinction between secretory androgen-dependent and lysosomal acid phosphatases. Activity of lysosomal acid phosphatase was increased after castration, while the activity of the secretory enzyme gradually decreased after androgen deprivation. None of the substrates tested was selectively hydrolyzed by either secretory or lysosomal acid phosphatase. Phenylphosphate, creatine phosphate and choline phosphate were found to be inappropriate substrates for histochemical purposes, however, reproducible results were obtained with alpha-naphthylphosphate, beta-glycerophosphate and p-nitrophenylphosphate. The method of isoelectric focussing (pH range 4.0--8.0) of enzymes with subsequent histochemical staining demonstrated lysosomal enzymes at pH 7.9 and 8.2 respectively. Small amounts of identical enzymes were found in liver, kidney, blood or epididymis. Secretory acid phosphatases were focussed at pH 5.5, 5.6, 5.65 and 7.15. Similar enzymes have been identified in epididymis, kidney, liver and pancreas. These results indicate that 1) at present no "specific" substrate for prostatic secretory or lysosomal acid phosphatases is available and 2) that no prostate-specific "prostatic acid phosphatase (PAP)" exists in the rat ventral prostate.