Acid Phosphatase in Human Female Genital Tract, A Histochemical and Biochemical Study.

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Abstract
Using fresh frozen sections and homogenates of tissues of the human female genital tract, considerable acid phosphatase activity was found histochemically and biochemically at pH 5, with glycerophosphate and some other phosphorylated derivatives, in the epithelial tissues (including glandular epithelium) of the vagina, uterus (including cervix) and fallopian tubes. By studies of activity at various pH levels from 2 to 11, with various substrates (ATP, phosphorylated carbohydrate intermediates, phenylphosphate), with other tissues (human prostate and rat liver), and with some inhibitors (0.01 and 0.001 [image] F-, 0.02 [image] tartrate, ethyl alcohol, acetone, and formaldehyde), the enzyme appears to resemble acid phosphatase of the human prostate and seminal fluid, although with less activity per unit wt. of tissue.

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