Purpose: To analyze water-soluble(WS) human lens proteins of fetus, adult and age-related cataract by two-dimensional IEF/SDSPAGE electrophoresis. Methods: DACM [ N- (7-Dimethylamino-4-methyl-3-coumarinyl) maleimide ]...Purpose: To analyze water-soluble(WS) human lens proteins of fetus, adult and age-related cataract by two-dimensional IEF/SDSPAGE 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. Eye Science 1999; 15:32-35.展开更多
文摘Purpose: To analyze water-soluble(WS) human lens proteins of fetus, adult and age-related cataract by two-dimensional IEF/SDSPAGE 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. Eye Science 1999; 15:32-35.
