THE MAJOR METABOLITE OF BENDAZAC INHIBITS THE GLYCOSYLATION OF SOLUBLE LENS PROTEINS - A POSSIBLE MECHANISM FOR A DELAY IN CATARACTOGENESIS

被引：16

作者：

LEWIS, BS ^{[1
]}

HARDING, JJ ^{[1
]}

机构：

[1] UNIV OXFORD,NUFFIELD LAB OPHTHALMOL,WALTON ST,OXFORD OX2 6AW,ENGLAND

来源：

EXPERIMENTAL EYE RESEARCH | 1988年 / 47卷 / 02期

关键词：

D O I：

10.1016/0014-4835(88)90005-X

中图分类号：

R77 [眼科学];

学科分类号：

100212 ;

摘要：

引用

页码：217 / 225

页数：9

共 15 条

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[7]

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[8] BENDAZAC PREVENTS CYANATE BINDING TO SOLUBLE LENS PROTEINS AND CYANATE-INDUCED PHASE-SEPARATION OPACITIES INVITRO - A POSSIBLE MECHANISM BY WHICH BENDAZAC COULD DELAY CATARACT [J].

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[9] NON-ENZYMATIC GLYCOSYLATION, SULFHYDRYL OXIDATION, AND AGGREGATION OF LENS PROTEINS IN EXPERIMENTAL SUGAR CATARACTS [J].

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[10] EFFECTS OF BENDAZAC L-LYSINE SALT ON X-RAY-INDUCED CATARACT IN THE RABBIT LENS [J].

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