Suppr超能文献

晶状体α-新蛋白

Lens alpha-neoproteins.

作者信息

Manski W, Malinowski K

机构信息

Department of Ophthalmology, College of Physicians and Surgeons, Columbia University, New York, N.Y.

出版信息

Ophthalmic Res. 1988;20(3):183-90. doi: 10.1159/000266584.

Abstract

The formation of lens alpha-neoprotein molecules which are built by the association of A and B subunit chains of alpha-crystallin but have a different quaternary structure than the native protein is a posttranslational process that progresses through the life span. Alpha-neoproteins occur regularly in all mature mammalian lenses tested. The mechanisms that have been identified for the formation of alpha neoproteins are imbalance in the biosynthesis of A- to B-chains, which leads to a ratio of less than 2A-chains to 1B-chain, and derivation of the chains after their initial association into native alpha-crystallin. In terms of quantity of neoproteins, no significant differences have been found between lenses with developing cataracts and normal control lenses of corresponding age. The possibility that there are structural differences between alpha-neoproteins in normal and cataractous lenses of the same age, as well as potential differences among alpha-neoproteins isolated from normal lenses of different ages, are presently under investigation.

摘要

晶状体α-新蛋白分子由α-晶状体蛋白的A和B亚基链缔合而成,但具有与天然蛋白质不同的四级结构,其形成是一个贯穿生命周期的翻译后过程。在所有测试的成熟哺乳动物晶状体中,α-新蛋白有规律地出现。已确定的α-新蛋白形成机制包括:A链与B链生物合成失衡,导致A链与B链的比例小于2:1;以及这些链在最初缔合成天然α-晶状体蛋白后发生衍生。就新蛋白的数量而言,患有白内障的晶状体与相应年龄的正常对照晶状体之间未发现显著差异。目前正在研究同一年龄的正常晶状体和白内障晶状体中的α-新蛋白之间是否存在结构差异,以及从不同年龄的正常晶状体中分离出的α-新蛋白之间是否存在潜在差异。

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验