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|Title:||Fractionation and characterization of oxytocinases in human semen||Authors:||Roy, A.C.
|Issue Date:||1989||Citation:||Roy, A.C., Sen, D.K., Ratnam, S.S. (1989). Fractionation and characterization of oxytocinases in human semen. Journal of Reproduction and Fertility 87 (1) : 163-168. ScholarBank@NUS Repository.||Abstract:||Two isoenzymes of oxytocinase activity were fractionated from human seminal plasma by acrylamide-agarose gel chromatography and partly characterized using S-benzyl-L-cysteine-p-nitroanilide (BCN) and L-leucine-p-nitroanilide (LN) separately as substrates. These isoenzymes appeared to be metallo-aminopeptidases with different elution volumes (90 ml and 150 ml), apparent molecular weights (unknown value and 300000) and pH optima (6.8 and 7.0 with BCN and 7.2 and 7.4 with LN), but with similar substrate affinity and thermal sensitivity, the susceptibility to EDTA, divalent metal ions, L-methionine, polypeptide hormones and prostaglandins. A comparison of the enzymic properties with pregnancy-associated oxytocinases suggests that seminal oxytocinases are related more closely to amniotic fluid isoenzymes than to pregnancy serum, placental and uterine isoenzymes.||Source Title:||Journal of Reproduction and Fertility||URI:||http://scholarbank.nus.edu.sg/handle/10635/131292||ISSN:||00224251|
|Appears in Collections:||Staff Publications|
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