Clinical Chemistry
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Clinical Chemistry 26: 254-257, 1980;
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Clinical Chemistry, Vol 26, 254-257, Copyright © 1980 by American Association for Clinical Chemistry

Rate of decrease of glutamyltransferase and acid phosphatase activities in the human vagina after coitus

WF Gohara

I studied the rate at which gamma-glutamyltransferase (EC 2.3.2.2) and acid phosphatase (EC 3.1.3.2) activities decrease in the healthy human vagina after coitus. Specimens from the coital and non-coital vagina, and from the rectum and buccal cavity, and pre-ejaculate lubricating fluid were also assayed for both enzymes. Prostatic acid phosphatase was determined with use of two substrates: thymolphthalein monophosphate and alpha-naphthyl phosphate (tartrate-inhibitable fraction). Glutamyltransferase was assayed with gamma-glutamyl-p- nitroanilide as substrate. All non-coital specimens were negative for glutamyltransferase activity; the activity of acid phosphatase varied with type of substrate and type of specimen. The equation y = a + (b/x) describes the decline in activity (y) of either acid phosphatase or glutamyltransferase in the vagina of healthy women post-coitally with time (x).




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Copyright © 1980 by the American Association for Clinical Chemistry.