Abstract
The acid phosphatase of mouse prostate was compared with that of other tissues, tumors, and cultured cells. Inhibitors of human prostatic acid phosphatase, such as tartrate and molybdate, inhibited the mouse prostatic enzyme only partially. Acid phosphatase from other mouse tissues (kidney, liver, cardiac and skeletal muscle) and tumors (sarcoma-180, adenocarcinoma-755, and the subcutaneous tumors induced by in vitro transformed prostate cells) were partially inhibited by 0.02 M tartrate also. Although there is some correlation between the prostatic origin of cells and the percentage of tartrate-inhibitable acid phosphatase (T i), it is not possible to conclude that T i is prostate-specific in the mouse. Histochemical studies with mouse prostate showed that acid phosphatase is localized predominantly in the epithelial cells of the acini. Mouse prostate tissue as well as the transformed prostate cells contained acid phosphatase that was not inhibited by tartrate. Acrylamide gel electrophoresis of mouse prostatic and kidney acid phosphatase was done under various conditions. No differences, with respect to electrophoretic mobilities or tartrate inhibition of the enzyme band after the electrophoresis, were found. It is concluded that acid phosphatase is not a suitable marker enzyme for mouse prostate cells.
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