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Radiolabelling of human haemoglobin using the 125I‐Bolton‐Hunter reagent is superior to oxidative iodination for conservation of the native structure of the labelled protein
Author(s) -
Frantzen F.,
DE Heggli,
Sundrehagen E.
Publication year - 1995
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1111/j.1470-8744.1995.tb00344.x
Subject(s) - labelling , reagent , chemistry , iodine , oxidative phosphorylation , halogenation , porphyrin , biochemistry , stereochemistry , organic chemistry
Both disruption of the native protein structure and oxidation of iron in the haem/iron(II)‐proto‐porphyrin‐IX residues were observed using the Iodo‐gen (1,3,4,6‐tetrachloro‐3 alpha,6 alpha‐diphenylglycouril) method in 125I‐labelling of haemoglobin. The reactions taking place affect the native structure of haemoglobin and result in a more acidic molecule. The detrimental effects were unaffected by the presence of iodine. Electrophoretic studies demonstrate that 125I‐labelling of haemoglobin using the Bolton‐Hunter reagent is the method of choice in order to preserve the native protein.