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Radiolabelling by tritium and [ 125 I]iodine of an angiotensin II related Peptide
Author(s) -
Pham P.,
Ramombordes C.,
Perret C.,
Ronco P.,
Budisavljevic M.,
Verroust P.,
Beaucourt J. P.
Publication year - 1991
Publication title -
journal of labelled compounds and radiopharmaceuticals
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.432
H-Index - 47
eISSN - 1099-1344
pISSN - 0362-4803
DOI - 10.1002/jlcr.2580290509
Subject(s) - chemistry , labelling , tritium , halogenation , tritium illumination , chloramine t , peptide , angiotensin ii , iodine monochloride , residue (chemistry) , amine gas treating , iodine , reagent , stereochemistry , receptor , radiochemistry , biochemistry , organic chemistry , physics , nuclear physics
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.