These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Heme peroxidase-catalyzed iodination of human angiotensins and the effect of iodination on angiotensin converting enzyme activity.
    Author: Bhuyan BJ, Mugesh G.
    Journal: Inorg Chem; 2008 Aug 04; 47(15):6569-71. PubMed ID: 18598023.
    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.
    [Abstract] [Full Text] [Related] [New Search]