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. 1984 Oct 1;223(1):221-7.
doi: 10.1042/bj2230221.

Conformational changes induced in bovine lens alpha-crystallin by carbamylation. Relevance to cataract

H T Beswick, J J Harding

Conformational changes induced in bovine lens alpha-crystallin by carbamylation. Relevance to cataract

H T Beswick et al. Biochem J. .

Abstract

Carbamylation of lens proteins may contribute to cataractogenesis in certain medical conditions where blood urea is elevated for prolonged periods. This paper reports on the effects of carbamylation on the physicochemical properties of one of the major lens structural proteins, alpha-crystallin. In particular it is shown that carbamylation alters the tertiary and secondary structure of the protein, leading to an increased reactivity of protein thiols, resulting in interchain disulphide bonding.

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