Aspirin prevents carbamylation of soluble lens proteins and prevents cyanate-induced phase separation opacities in vitro: A possible mechanism by which aspirin could prevent cataract-Reference-Cited by-同舟云学术

Aspirin prevents carbamylation of soluble lens proteins and prevents cyanate-induced phase separation opacities in vitro: A possible mechanism by which aspirin could prevent cataract

Published:1985-02 Issue:2 Volume:40 Page:297-311
ISSN:0014-4835
Container-title:Experimental Eye Research
language:en
Short-container-title:Experimental Eye Research

Author:

Crompton Mark,Rixon Ken C.,Harding John J.

Publisher

Elsevier BV

Subject

Cellular and Molecular Neuroscience,Sensory Systems,Ophthalmology

Reference36 articles.

1. Non-enzymic modification of human lens proteins in vitro in relation to cataractogenesis;Beswick;Biochem. Soc. Trans.,1982

2. Conformational changes induced in bovine alpha crystallin by protein carbamylation: relevance to cataract;Beswick;Biochem. J.,1984

3. Growing insight into the structure of β-crystallin;Bloemendal;Ophthalmic Res.,1974

4. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding;Bradford;Anal. Biochem.,1976

5. The effects of glycols, aldehydes and acrylamide on phase separation and opacification in the calf lens;Clark;Invest. Ophthalmol.,1980

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