使用等电聚焦对晶状体γ-晶体蛋白进行的比较研究。

A comparative study of lens gamma crystallins using isoelectric focusing.

作者信息

Zigman S, Schultz J, Yulo T

出版信息

Comp Biochem Physiol B. 1983;75(3):425-7. doi: 10.1016/0305-0491(83)90352-8.

Abstract

The isoelectric points of gamma crystallins of the lenses of rats, dogfish, calves, and humans differ, with a range of pH 8.87-6.80. In each species, one gamma crystallin component with an isoelectric point at pH 7.5 is present, but at differing levels. Amino acid compositions of this component were similar among these four species. All pH 7.5 isoelectric point proteins crossreact immunochemically. A common messenger RNA must be present for this gamma crystallin in all of these species.

摘要

大鼠、角鲨、小牛和人类晶状体的γ-晶状体蛋白的等电点各不相同，范围在pH 8.87至6.80之间。在每个物种中，都存在一种等电点为pH 7.5的γ-晶状体蛋白成分，但含量不同。这一成分在这四个物种中的氨基酸组成相似。所有等电点为pH 7.5的蛋白质都能发生免疫交叉反应。在所有这些物种中，这种γ-晶状体蛋白必定存在一种共同的信使核糖核酸。