Bhuyan, Bhaskar J. ; Mugesh, Govindasamy (2008) Heme peroxidase-catalyzed iodination of human angiotensins and the effect of iodination on angiotensin converting enzyme activity Inorganic Chemistry, 47 (15). pp. 6569-6571. ISSN 0020-1669
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Official URL: http://pubs.acs.org/doi/abs/10.1021/ic800395k
Related URL: http://dx.doi.org/10.1021/ic800395k
Abstract
The heme peroxidase-catalyzed iodination of human angiotensins I and II is described. It is observed that lactoperoxidase (LPO) can effectively and selectively iodinate the tyrosyl residues in angiotensin peptides. The thiourea/thiouracil-based peroxidase inhibitors effectively inhibit the iodination reactions, indicating that iodination is an enzymatic reaction and the mechanism of iodination is similar to that of peroxidase-catalyzed iodination of thyroglobulin. This study also shows that the monoiodo Ang I is a better substrate for the angiotensin converting enzyme than the native peptide.
| Item Type: | Article |
|---|---|
| Source: | Copyright of this article belongs to American Chemical Society. |
| ID Code: | 79311 |
| Deposited On: | 25 Jan 2012 06:31 |
| Last Modified: | 25 Jan 2012 06:31 |
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