RADIOLABELING OF HUMAN HEMOGLOBIN USING THE I-125 BOLTON-HUNTER REAGENT IS SUPERIOR TO OXIDATIVE IODINATION FOR CONSERVATION OF THE NATIVE STRUCTURE OF THE LABELED PROTEIN
F. Frantzen et al., RADIOLABELING OF HUMAN HEMOGLOBIN USING THE I-125 BOLTON-HUNTER REAGENT IS SUPERIOR TO OXIDATIVE IODINATION FOR CONSERVATION OF THE NATIVE STRUCTURE OF THE LABELED PROTEIN, Biotechnology and applied biochemistry, 22, 1995, pp. 161-167
Both disruption of the native protein structure and oxidation of iron
in the haem/iron(II)-proto-porphyrin-IX residues were observed using t
he Iodo-gen (1,3,4,6-tetrachloro-3 alpha,6 alpha-diphenylglycouril) me
thod in I-125-labelling of haemoglobin. The reactions taking place aff
ect the native structure of haemoglobin and result in a more acidic mo
lecule. The detrimental effects were unaffected by the presence of iod
ine. Electrophoretic studies demonstrate that I-125-labelling of haemo
globin using the Bolton-Hunter reagent is the method of choice in orde
r to preserve the native protein.