Radiolabelling of human haemoglobin using the ~(125)I- Bolton-Hunter reagent is superior to oxidative iodination for conservation of the native structure of the labelled protein

摘要

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-3α,6α-diphenylglycouril) method in ~(125)I-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 ~(125)I-labelling of haemoglobin using the Bolton-Hunter reagent is the method of choice in order to preserve the native protein.