Evans R W, Williams J
Biochem J. 1980 Sep 1;189(3):541-6. doi: 10.1042/bj1890541.
The denaturation of transferrin by urea has been studied by (a) electrophoresis in polyacrylamide gels incorporating a urea gradient, (b) measurements of the loss of iron-binding capacity and (c) u.v. difference spectrometry. In human serum transferrin and hen ovotransferrin the N-terminal and C-terminal domains of the iron-free protein were found to denature at different urea concentrations.
(a)在含有尿素梯度的聚丙烯酰胺凝胶中进行电泳,(b)测量铁结合能力的丧失,以及(c)紫外差光谱法。在人血清转铁蛋白和鸡卵转铁蛋白中,发现无铁蛋白的N端和C端结构域在不同的尿素浓度下会发生变性。