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|Title:||Relative effects of oxytocin, vasopressin and angiotensin II on the hydrolysis of S-benzyl-L-cysteine-p-nitroanilide and L-leucine-p-nitroanilide by pregnancy-related oxytocinases|
|Authors:||Roy, A.C.C. |
|Citation:||Roy, A.C.C., Yeang, M., Kottegoda, S.R., Ratnam, S.S. (1986). Relative effects of oxytocin, vasopressin and angiotensin II on the hydrolysis of S-benzyl-L-cysteine-p-nitroanilide and L-leucine-p-nitroanilide by pregnancy-related oxytocinases. IRCS Medical Science 14 (8) : 830-831. ScholarBank@NUS Repository.|
|Abstract:||Oxytocinase (EC 22.214.171.124), a pregnancy-related oxytocin-inactivating α-aminoacyl hydrolase, also has the ability to degrade vasopressin, angiotensin II and some synthetic peptides. Two such peptides, S-benzyl-L-cysteine-p-nitroanilide (BCN) and L-leucine-p-nitroanilide (LN) with proven substrate specificity, have been widely used to study oxytocinase activity in vitro. However, the relative binding affinity of these and the natural octapeptide substrates with oxytocinase or its various isoenzymes is not known. In this study, it has been demonstrated that the polypeptide hormones competitively inhibit the hydrolysis of BCN or LN by oxytocinases from serum, placenta, uterus and amniotic fluid in a differential manner. Judged by the Ki values of the octapeptides which negatively reflect their inactivation or hydrolysis by oxytocinases, it is concluded that the enzyme component which inactivates angiotensin II is predominant in all the samples tested followed by the oxytocin and vasopressin-inactivating components.|
|Source Title:||IRCS Medical Science|
|Appears in Collections:||Staff Publications|
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