CONFORMATIONAL-CHANGES INDUCED IN BOVINE LENS ALPHA-CRYSTALLIN BY CARBAMYLATION - RELEVANCE TO CATARACT
CONFORMATIONAL-CHANGES INDUCED IN BOVINE LENS ALPHA-CRYSTALLIN BY CARBAMYLATION - RELEVANCE TO CATARACT
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DOI：
10.1042/bj2230221
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发表时间：
1984-01-01
影响因子：
4.1
通讯作者：
HARDING, JJ
中科院分区：
文献类型：
--
作者：
BESWICK, HT;HARDING, JJ
透镜蛋白的氨甲酰化可能在血尿素长时间升高的某些医学病症中促成白内障发生。氨甲酰化对主要透镜结构蛋白之一α-β-葡聚糖的物理化学性质的影响晶体蛋白。特别是，氨甲酰化改变了蛋白质的三级和二级结构，导致蛋白质巯基的反应性增加，导致链间二硫键。
Cabamylation of lens proteins may contribute to cataractogenesis in certain medical conditions where blood urea is elevated for prolonged period. The effects of carbamylation on the physicochemical properties of one of the major lens structural proteins, .alpha.-crystallin, are reported. In particular, carbamylation alters the tertiary and secondary structure of the protein, leading to an increased reactivity of protein thiols, resulting in interchain disulfide bonding.