Frantzen F, Heggli D E, Sundrehagen E
Axis Nord AS, Mørkved, Norway.
Biotechnol Appl Biochem. 1995 Oct;22(2):161-7.
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.
在血红蛋白的¹²⁵I标记过程中，采用碘酰法（1,3,4,6 - 四氯 - 3α,6α - 二苯基甘脲）时，观察到天然蛋白质结构的破坏以及血红素/亚铁原卟啉 - IX残基中铁的氧化。发生的这些反应会影响血红蛋白的天然结构，并导致分子酸性增强。碘的存在不会影响这些有害作用。电泳研究表明，为了保留天然蛋白质，使用博尔顿 - 亨特试剂对血红蛋白进行¹²⁵I标记是首选方法。
