Conformational changes induced in bovine lens α-crystallin by carbamylation. Relevance to cataract
- 1 October 1984
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 223 (1) , 221-227
- https://doi.org/10.1042/bj2230221
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.This publication has 2 references indexed in Scilit:
- X-ray analysis of the eye lens protein γ-II crystallin at 1·9 Å resolutionJournal of Molecular Biology, 1983
- The Optical Rotatory Dispersion and Circular Dichroism of Calf Lens α-CrystallinJournal of Biological Chemistry, 1967