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Role of gamma crystallins on the insolubilization of human soluble lens proteins

Kabasawa, I.; Yokota, T.; Kodama, T.; Kodama, T.; Watanabe, M.; Kimura, M.

Nippon Ganka Gakkai Zasshi 91(1): 140-144

1987

ISSN/ISBN: 0029-0203
PMID: 3591572
Document Number: 294329
The increase of .gamma.H crystallin with age was apparent in human normal and premature lens soluble proteins on gel filtration of Sephadex G-75 superfine column chromatography. However, the decrease of .gamma.H crystallin was found in the mature, especially brown colored cataractous lenses. In the two dimensional electrophoretic pattern, the decrease of the neutral to acidic .gamma.H crystallin spots was observed in the human mature lens soluble proteins. The pattern changes observed in the two dimensional electrophoresis of human mature lens soluble proteins was generally similar to those observed in the carboxymethylation of human premature lens soluble proteins. The decrease of .gamma.H crystallin in the human mature lens soluble proteins could be caused by the S-S bond formation during cataractogenesis.

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