Griess G A, Zigman S, Yulo T
Mol Cell Biochem. 1976 Jul 30;12(1):9-14. doi: 10.1007/BF01731898.
Variations in size and charge of calf lens proteins, particularly gamma crystallins, were studied by polyacrylamide gel electrophoresis. Exposure of gamma crystallins to near-UV light in the presence of L-tryptophan produces species of higher electrophoretic mobility and higher retardation. Treatment with urea and sulfonation also produced changes in the retardation co-efficient. The increase of retardation co-efficient of gamma crystallin is interpreted to be a result of conformational changes. Gamma crystallins are particularly sensitive to photo-modification, and this process may be associated with age-related changes in the lens.
通过聚丙烯酰胺凝胶电泳研究了小牛晶状体蛋白，特别是γ-晶状体蛋白在大小和电荷上的变化。在L-色氨酸存在的情况下，γ-晶状体蛋白暴露于近紫外光会产生具有更高电泳迁移率和更高阻滞作用的物种。用尿素和磺化处理也会导致阻滞系数发生变化。γ-晶状体蛋白阻滞系数的增加被解释为构象变化的结果。γ-晶状体蛋白对光修饰特别敏感，这个过程可能与晶状体中与年龄相关的变化有关。
