STUDIES OF GLYCERYLPHOSPHORYLCHOLINE DIESTERASE IN THE FEMALE REPRODUCTIVE TRACT

Publisher Website
Google Scholar
Abstract
The occurrence of an enzyme which hydrolyses seminal glycerylphosphorylcholine (GPC) has been demonstrated in uterine rinsings of the ewe, cow, sow, rat and mouse. The products of the breakdown of GPC by rinsings of the ewe''s uterus, which also contain an active phosphatase, are glycerol, inorganic phosphate and choline. Lower levels of GPC diesterase activity were also found in the cervical and oviduct fluids of the ewe. No diesterase activity could be demonstrated in the follicular fluid of the ewe, which contained appreciable concentrations of lactic acid and glucose. Secretion of the diesterase in the ewe is influenced by the stage of the estrous cycle independently of changes in other luminal fluid proteins or the wet weight of the uterus. Diesterase activity in uterine rinsings of the ewe is greatest at the time of ovulation. The evidence indicates that the enzyme of the uterine tissue and is not of bacterial origin. The optimal pH is 7.7 and the enzyme is not inhibited by fluoride or eserine.