Heme Peroxidase-Catalyzed Iodination of Human Angiotensins and the Effect of Iodination on Angiotensin Converting Enzyme Activity

Bhuyan, Bhaskar J and Mugesh, Govindasamy (2008) Heme Peroxidase-Catalyzed Iodination of Human Angiotensins and the Effect of Iodination on Angiotensin Converting Enzyme Activity. In: Inorganic Chemistry, 47 (15). pp. 6569-6571.

PDF heme.pdf - Published Version Restricted to Registered users only Download (232Kb) | Request a copy

Abstract

The heme peroxidase-catalyzed iodination of human angiotensins I and II is described. It is observed that lactoperoxiclase (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:	Journal Article
Additional Information:	Copyright of this article belongs to American Chemical Society.
Department/Centre:	Division of Chemical Sciences > Inorganic & Physical Chemistry
Date Deposited:	07 Oct 2008 06:28
Last Modified:	19 Sep 2010 04:51
URI:	http://eprints.iisc.ernet.in/id/eprint/16159

Actions (login required)

View Item