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Peptidic hormone interactions at the molecular level‐preparation of highly labelled 3 H oxytocin
Author(s) -
Morgat J. L.,
Hung Lam Thanh,
Cardinaud R.,
Fromageot P.,
Bockaert J.,
Imbert M.,
Morel F.
Publication year - 1970
Publication title -
journal of labelled compounds
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.432
H-Index - 47
eISSN - 1099-1344
pISSN - 0022-2135
DOI - 10.1002/jlcr.2590060308
Subject(s) - oxytocin , labelling , tritium , chemistry , halogenation , hormone , iodine , specific activity , peptide , reagent , disulfide bond , stereochemistry , radiochemistry , biochemistry , organic chemistry , endocrinology , biology , enzyme , physics , nuclear physics
The tritium labelling of oxytocin has been attained by a two step procedure. First, di‐iodo oxytocin is prepared. After a survey of various iodination reagents, ICI has been selected as it reacts much more rapidly with the tyrosyl ring than with the disulfide bridge, which under mild conditions remains unaffected. The di‐iodo derivative, nevertheless, has lost most or all of its biological activity. Catalytic substitution of the peptide bound iodine by tritium results in labelling the hormone and in restoration of the biological activity. The 3 H oxytocin obtained retains 90 % of its hydrosmotic activity and about 65 % of its avian depressor activity. Its specific radioactivity reaches 36 Ci/mMole, a value allowing further studies of the hormone at a molecular level.