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.
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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|
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