二维电泳中不同年龄人晶状体晶状体蛋白的分布及其巯基含量
Distribution of human lens crystallins and their sulphydryl contents of different age in two-dimension electrophoresis.
作者信息
Wu Y, Pan S, Li S, Huang Q, Fu S C
机构信息
National Ophthalmologiced Laboratories, Ministry of Public Health, Zhongshan Ophthalmic Center, Sun Yat-sen University of Medical Sciences, Guangzhou, China.
出版信息
Yan Ke Xue Bao. 1999 Mar;15(1):32-5.
PURPOSE
To analyze water-soluble (WS) human lens proteins of fetus, adult and age-related cataract by two-dimensional IEF/SDS-PAGE electrophoresis.
METHODS
DACM [N-(7-Dimethylamino-4-methyl-3-coumarinyl) maleimide] was used to determine the lens proteins sulphydryl (SH) content.
RESULT
Protein SH contents in WS lens proteins have no significant difference among fetus, adult and age-related cataract lens. This is different from the relative published results obtained in lens proteins of animal cataract model using similar SH detecting methods.
CONCLUSIONS
IEF/SDS-PAGE electrophoresis demonstrated that there were much more fragmentation of crystallins during lens development and cataractogenic process. It is suggested that this phenomenon is likely to be due to further conformational changes in the fragmented cyrstallins during aging and cataractogenic process.
目的
通过二维IEF/SDS - PAGE电泳分析胎儿、成人及年龄相关性白内障的水溶性（WS）人晶状体蛋白。
方法
使用DACM [N -（7 - 二甲基氨基 - 4 - 甲基 - 3 - 香豆素基）马来酰亚胺]测定晶状体蛋白巯基（SH）含量。
结果
WS晶状体蛋白中的蛋白质SH含量在胎儿、成人及年龄相关性白内障晶状体之间无显著差异。这与使用类似SH检测方法在动物白内障模型晶状体蛋白中获得的相对已发表结果不同。
结论
IEF/SDS - PAGE电泳表明，在晶状体发育和致白内障过程中，晶状体蛋白有更多的片段化。提示这种现象可能是由于片段化的晶状体蛋白在衰老和致白内障过程中进一步的构象变化所致。
Zotero 插件