Johnson G B
Biochem Genet. 1977 Aug;15(7-8):665-93. doi: 10.1007/BF00484097.
Enzyme polymorphism was characterized among the proteins of 14 loci of Coliae meadii by replicate electrophoresis in polyacrylamide gels of differing pore size. The results reveal a large number of variants, with a very skewed frequency distribution. A large fraction of the variants cannot be differentiated by electrophoresis in 5--7% acrylamide gels. This gel sieving approach permits an estimate of the relative contributions of charge and of conformation to electrophoretic mobility. Many of the variant proteins do not differ in charge. Most variants exhibit different degrees of interaction with the gel and presumably differ in conformation.
通过在不同孔径的聚丙烯酰胺凝胶中进行重复电泳，对米氏柯利虫（Coliae meadii）14个位点的蛋白质中的酶多态性进行了表征。结果显示出大量的变体，其频率分布非常不均衡。很大一部分变体在5%-7%丙烯酰胺凝胶中无法通过电泳区分。这种凝胶筛分方法能够估计电荷和构象对电泳迁移率的相对贡献。许多变体蛋白质在电荷上没有差异。大多数变体与凝胶表现出不同程度的相互作用，推测其构象也有所不同。
