| Distribution of Human Lens Crystallins and Their Sulphydryl Contents of Different Age in Two—dimension Electrophoresis |
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| 引用本文： | Yi Wu S.C.Joseph Fu 等. Distribution of Human Lens Crystallins and Their Sulphydryl Contents of Different Age in Two—dimension Electrophoresis[J]. 眼科学报, 1999, 15(1): 32-35 |
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| 作者姓名： | Yi Wu S.C.Joseph Fu 等 |
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| 摘 要： | 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.
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| 关 键 词： | 眼 晶体状 白内障 巯基 双向电泳 |
Distribution of Human Lens Crystallins and Their Sulphydryl Contents of Different Age in Two-dimension Electrophoresis |
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| Y Wu,S Pan,S Li,Q Huang,S C Fu. Distribution of Human Lens Crystallins and Their Sulphydryl Contents of Different Age in Two-dimension Electrophoresis[J]. Eye science, 1999, 15(1): 32-35 |
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| Authors: | Y Wu S Pan S Li Q Huang S C Fu |
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| Affiliation: | National Ophthalmologiced Laboratories, Ministry of Public Health, Zhongshan Ophthalmic Center, Sun Yat-sen University of Medical Sciences, Guangzhou, China. |
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| Abstract: | 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. |
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| Keywords: | lens crystallins cataract sulphydryl two-dimensional electrophoresis |
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