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Peptide and protein labelling with iodine, iodine monochloride reaction with aqueous solution of L‐tyrosine, L‐histidine, L‐histidine‐peptides, and his effect on some simple disulfide bridges
Author(s) -
Hung Lam Thanh,
Fermandjian S.,
Morgat J. L.,
Fromageot P.
Publication year - 1974
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.2590100102
Subject(s) - chemistry , iodine monochloride , histidine , tyrosine , peptide , halogenation , aqueous solution , iodine , hydrolysis , circular dichroism , labelling , combinatorial chemistry , stereochemistry , organic chemistry , biochemistry , enzyme
Iodinated peptides or proteins ( 125 I, 131 I) are used as tracers for radioimmono assays and for detection in biological systems. The labelling takes place on the aromatic side chains. However, when disulfide bridges are present, iodination must be carried out under conditions preventing their degradation. The rate of iodination of L‐tyrosine, L‐histidine and L‐histidine containing peptides by iodine monochloride (ICI) are studied by spectroscopy. Free hitidine increases the hydrolysis rate of aqueous solution of ICI. The interactions between ICI and some simple disulfide are investigated by circular dichroism measurements. These reactions are presented as models for degradation of disulfide bridges in peptide or protein during the iodination process.