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.
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.
Frantzen
F
F
Axis Nord AS, Mørkved, Norway.
Heggli
D E
DE
Sundrehagen
E
E
D004591:Electrophoresis, Polyacrylamide Gel; D006454:Hemoglobins / Q000737:chemistry*; D006801:Humans; D007202:Indicators and Reagents / Q000737:chemistry*; D007457:Iodine Radioisotopes / Q000737:chemistry*; D007525:Isoelectric Focusing; D010084:Oxidation-Reduction; D011487:Protein Conformation; D014508:Urea / Q000031:analogs & derivatives* / Q000737:chemistry
D006454:Hemoglobins; D007202:Indicators and Reagents; D007457:Iodine Radioisotopes; C012385:1,3,4,6-tetrachloro-3 alpha,6 alpha-diphenylglycoluril; D014508:Urea