Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/134231
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. 
Yeang, M.
Kottegoda, S.R.
Ratnam, S.S. 
Issue Date: 1986
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 3.4.11.3), 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
URI: http://scholarbank.nus.edu.sg/handle/10635/134231
ISSN: 03056651
Appears in Collections:Staff Publications

Show full item record
Files in This Item:
There are no files associated with this item.

Page view(s)

12
checked on Dec 14, 2018

Google ScholarTM

Check


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.