Radiolabelling by tritium and [125I]iodine of an angiotensin II related Peptide

✍ Scribed by P. Pham; C. Ramombordes; C. Perret; P. Ronco; M. Budisavljevic; P. Verroust; J. P. Beaucourt

• Book ID: 102374827
• Publisher: John Wiley and Sons
• Year: 1991
• Tongue: French
• Weight: 313 KB
• Volume: 29
• Category: Article
• ISSN: 0022-2135
• DOI: 10.1002/jlcr.2580290509

✦ Synopsis

Abstract

We describe the ^3^H‐ and ^125^I‐ labelling of Glu‐Gly‐Val‐Tyr‐Val‐His‐Pro‐Val, (hIIA), an octapeptide encoded by an RNA strand complementary to the human angiotensin II (AII) mRNA.

The labelling of this peptide with ^125^I was performed by two ways : 1/ Mono‐iodination of the Tyr residue, using Na^125^I in the presence of Chloramine T; 2/ Coupling of the [^125^I]Bolton‐Hunter reagent to the terminal amine group of the octapeptide.

The synthesis of the tritiated (3,5‐^3^H~2~‐Tyr^4^)octapeptide was achieved by a two step synthesis : di‐iodination of the peptide followed by its catalytic dehalogenation in the presence of tritium gas.

The compounds obtained inhibited the binding of AII to its receptors or antibodies but showed no direct binding to these proteins, suggesting no competition between AII and hIIA for these protein binding sites.