Garadi R, Katar M, Maisel H
Exp Eye Res. 1983 Jun;36(6):859-69. doi: 10.1016/0014-4835(83)90039-8.
Two-dimensional analyses of the chick lens water-soluble and water-insoluble proteins were conducted according to the method of O'Farrell (1975). The results define the isoelectric properties of the water-soluble and the urea-soluble polypeptides and demonstrate differences in composition for cortical and nuclear proteins. Chick lens vimentin consists of at least two isoelectric variants, and its breakdown products were identified. Chick lens actin is primarily of the gamma-type. The 47 K polypeptide specific for fiber cells shows considerable charge heterogeneity, and its most acidic component is found primarily in the nuclear fiber cells. This study also shows that apparently single bands resolved by one-dimensional SDS-polyacrylamide gel electrophoresis of the urea-soluble fraction consists of different proteins, and that the composition of such bands may further be altered by ph. This is especially relevant to the composition of the 47 and 50 K bands.
根据奥法雷尔（1975年）的方法，对鸡晶状体的水溶性和水不溶性蛋白质进行了二维分析。结果确定了水溶性和尿素溶性多肽的等电性质，并证明了皮质蛋白和核蛋白在组成上的差异。鸡晶状体波形蛋白至少由两种等电变体组成，并鉴定出其降解产物。鸡晶状体肌动蛋白主要是γ型。纤维细胞特有的47K多肽显示出相当大的电荷异质性，其最酸性的成分主要存在于核纤维细胞中。这项研究还表明，尿素溶性部分经一维SDS-聚丙烯酰胺凝胶电泳分离出的明显单一的条带由不同的蛋白质组成，并且这些条带的组成可能会因pH值而进一步改变。这与47K和50K条带的组成尤其相关。
