CYTO-CHEMISTRY AND BIOCHEMISTRY OF ACID-PHOSPHATASES .1. CYTO-CHEMISTRY AND ISOELECTRIC-FOCUSING OF ACID-PHOSPHATASES OF THE RAT VENTRAL PROSTATE

  • 1 January 1980
    • journal article
    • research article
    • Vol. 67  (1) , 99-111
Abstract
Acid phosphatases of the rat ventral prostate were studied cytochemically using different substrates. The results were compared to findings on isoelectric focusing 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. No substrate tested was selectively hydrolyzed by either secretory or lysosomal acid phosphatase. Phenylphosphate, creatine phosphate and choline phosphate were inappropriate substrates for histochemical purposes; reproducible results were obtained with .alpha.-naphthylphosphate, .beta.-glycerophosphate and p-nitrophenylphosphate. The method of isoelectric focusing (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 were identified in epididymis, kidney, liver and pancreas. At present no specific substrate for prostatic secretory or lysosomal acid phosphatases is available and apparently no prostate-specific prostatic acid phosphatase (PAP) exists in the rat ventral prostate.

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