人晶状体中γS-晶状体蛋白上谷胱甘肽混合二硫化物形成反应位点的鉴定。
The identification of a reaction site of glutathione mixed-disulphide formation on gammaS-crystallin in human lens.
作者信息
Craghill Jane, Cronshaw Andrew D, Harding John J
机构信息
Nuffield Laboratory of Ophthalmology, University of Oxford, Walton Street, Oxford OX2 6AW, UK.
出版信息
Biochem J. 2004 May 1;379(Pt 3):595-600. doi: 10.1042/BJ20031367.
The glutathionylation of human lens proteins was examined by Western-blot analysis with an anti-GSH antibody and scanning. Several different glutathionylated proteins were observed, and a 47 kDa band was of particular interest. This band did not appear after SDS/PAGE under reducing conditions, suggesting that it was a glutathionylated fraction. The 47 kDa band was found principally in the outer part of the lens, the cortex, but not in the lens nucleus where older proteins are present. The 47 kDa component was composed of betaB1-, betaB2- and gammaS-crystallin, with the gammaS-crystallin having glutathione bound at Cys-82 and at Cys-22, Cys-24 or Cys-26. We conclude that when glutathione becomes bound to gammaS-crystallin, it causes it to bind in turn to the beta-crystallin polypeptides to form a dimer.
通过使用抗谷胱甘肽（GSH）抗体的蛋白质免疫印迹分析和扫描，检测了人晶状体蛋白的谷胱甘肽化修饰情况。观察到几种不同的谷胱甘肽化修饰的蛋白质，其中一条47 kDa的条带尤为引人关注。在还原条件下进行十二烷基硫酸钠/聚丙烯酰胺凝胶电泳（SDS/PAGE）后，这条带未出现，这表明它是一个谷胱甘肽化修饰的组分。47 kDa的条带主要存在于晶状体的外层，即皮质，但在含有较老蛋白质的晶状体核中未发现。47 kDa的组分由βB1 -、βB2 -和γS -晶状体蛋白组成，γS -晶状体蛋白在半胱氨酸（Cys）- 82以及Cys - 22、Cys - 24或Cys - 26处结合有谷胱甘肽。我们得出结论，当谷胱甘肽与γS -晶状体蛋白结合时，会使其进而与β -晶状体蛋白多肽结合形成二聚体。
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