Evans R W, Williams J, Moreton K
Biochem J. 1982 Jan 1;201(1):19-26. doi: 10.1042/bj2010019.
Screening of human serum samples by polyacrylamide-gel electrophoresis in the presence of 6 M-urea revealed an individual who is heterozygous for a variant transferrin. The variant transferrin is able to bind two atoms of iron, but the iron in the C-terminal binding site is bound abnormally, as judged by its spectral properties, and is dissociated from the protein on electrophoresis in the presence of 6 M-urea. The iron-free C-terminal domain of the variant protein is less stable than normal to thermal and urea denaturation. Structural changes in the variant protein have not yet been characterized.
在6M尿素存在的情况下,通过聚丙烯酰胺凝胶电泳对人血清样本进行筛查,发现一名个体为变异转铁蛋白的杂合子。该变异转铁蛋白能够结合两个铁原子,但根据其光谱特性判断,C端结合位点的铁结合异常,并且在6M尿素存在的情况下电泳时会从蛋白质上解离。变异蛋白的无铁C端结构域对热和尿素变性的稳定性低于正常情况。变异蛋白的结构变化尚未得到表征。