Conformational changes induced in bovine lens alpha-crystallin by carbamylation. Relevance to cataract.
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.
D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D003459:Crystallins / Q000378:metabolism*; D003485:Cyanates / Q000494:pharmacology*; D004591:Electrophoresis, Polyacrylamide Gel; D011487:Protein Conformation; D013438:Sulfhydryl Compounds / Q000032:analysis; D014783:Viscosity
D003459:Crystallins; D003485:Cyanates; D013438:Sulfhydryl Compounds; C005057:isocyanic acid