Distribution of human lens crystallins and their sulphydryl contents of different age in two-dimension electrophoresis.
OBJECTIVE
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.


RESULTS
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.
Wu
Y
Y
National Ophthalmologiced Laboratories, Ministry of Public Health, Zhongshan Ophthalmic Center, Sun Yat-sen University of Medical Sciences, Guangzhou, China.
Pan
S
S
Li
S
S
Huang
Q
Q
Fu
S C
SC
D000328:Adult; D000367:Age Factors; D000368:Aged; D000369:Aged, 80 and over; D002386:Cataract / Q000378:metabolism; D003459:Crystallins / Q000378:metabolism*; D015180:Electrophoresis, Gel, Two-Dimensional; D005260:Female; D005333:Fetus; D006801:Humans; D007908:Lens, Crystalline / Q000378:metabolism; D008297:Male; D008875:Middle Aged; D013438:Sulfhydryl Compounds / Q000032:analysis*
D003459:Crystallins; D013438:Sulfhydryl Compounds