• 文献检索
  • 文档翻译
  • 深度研究
  • 学术资讯
  • Suppr Zotero 插件Zotero 插件
  • 邀请有礼
  • 套餐&价格
  • 历史记录
应用&插件
Suppr Zotero 插件Zotero 插件浏览器插件Mac 客户端Windows 客户端微信小程序
定价
高级版会员购买积分包购买API积分包
服务
文献检索文档翻译深度研究API 文档MCP 服务
关于我们
关于 Suppr公司介绍联系我们用户协议隐私条款
关注我们

Suppr 超能文献

核心技术专利:CN118964589B侵权必究
粤ICP备2023148730 号-1Suppr @ 2026

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

人类白内障形成过程中晶状体膜蛋白的分子间二硫键结合

Intermolecular disulfide bonding of lens membrane proteins during human cataractogenesis.

作者信息

Takemoto L J, Hansen J S

出版信息

Invest Ophthalmol Vis Sci. 1982 Mar;22(3):336-42.

PMID:7061206
Abstract

Two-dimensional diagonal electrophoresis has been used to characterize intermolecular disulfide bonding of membrane proteins from lenses of cataractous and normal patients. A component of approximately 18,000 daltons, linked via intermolecular disulfide bonding, was found in membrane preparations from 10 of 17 cataracts studied. In comparison, membrane from only 1 of 12 normal lenses of approximately the same age range was found to contain intermolecular disulfide bonding of a component of similar molecular weight. Treatment of normal lens with the oxidizing agents cupric sulfate and 1,10-phenanthroline resulted in intermolecular disulfide bonding of the 18K component in a manner similar to that found in cataractous lenses. Together these results demonstrate that human cataractogenesis is many times accompanied by intermolecular disulfide bonding of a membrane component of 18K and suggest that this intermolecular bonding may be the result of the previously reported oxidative insult of the lens during human cataract formation.

摘要

二维对角线电泳已被用于表征白内障患者和正常患者晶状体膜蛋白的分子间二硫键结合情况。在研究的17例白内障患者中的10例的膜制剂中发现了一种通过分子间二硫键连接的约18,000道尔顿的成分。相比之下,在年龄范围大致相同的12例正常晶状体中,只有1例的膜含有分子量相似的成分的分子间二硫键结合。用氧化剂硫酸铜和1,10-菲咯啉处理正常晶状体,会导致18K成分发生分子间二硫键结合,其方式与在白内障晶状体中发现的类似。这些结果共同表明,人类白内障形成过程中多次伴随着18K膜成分的分子间二硫键结合,并表明这种分子间结合可能是先前报道的人类白内障形成过程中晶状体氧化损伤的结果。

相似文献

1
Intermolecular disulfide bonding of lens membrane proteins during human cataractogenesis.人类白内障形成过程中晶状体膜蛋白的分子间二硫键结合
Invest Ophthalmol Vis Sci. 1982 Mar;22(3):336-42.
2
Characterization of disulfide-linked crystallins associated with human cataractous lens membranes.与人类白内障晶状体膜相关的二硫键连接的晶状体蛋白的特性分析。
Invest Ophthalmol Vis Sci. 1988 Jan;29(1):145-9.
3
Characterization of water-insoluble proteins in normal and cataractous human lens.正常和白内障人晶状体中不溶性蛋白质的特性分析
Jpn J Ophthalmol. 1990;34(2):216-24.
4
Multi-crystallin complexes exist in the water-soluble high molecular weight protein fractions of aging normal and cataractous human lenses.多晶体蛋白复合物存在于正常衰老和患白内障的人晶状体的水溶性高分子量蛋白质组分中。
Exp Eye Res. 2008 Oct;87(4):356-66. doi: 10.1016/j.exer.2008.07.001. Epub 2008 Jul 10.
5
Transition metal-catalyzed oxidation of ascorbate in human cataract extracts: possible role of advanced glycation end products.过渡金属催化人白内障提取物中抗坏血酸的氧化:晚期糖基化终产物的可能作用。
Invest Ophthalmol Vis Sci. 2000 May;41(6):1473-81.
6
Deamidation and disulfide bonding in human lens gamma-crystallins.人晶状体γ-晶状体蛋白中的脱酰胺作用和二硫键结合
Exp Eye Res. 1998 Sep;67(3):301-12. doi: 10.1006/exer.1998.0530.
7
Proteomic analysis of water insoluble proteins from normal and cataractous human lenses.正常和白内障人晶状体水不溶性蛋白质的蛋白质组学分析。
Mol Vis. 2007 Sep 14;13:1680-94.
8
Quantitation of membrane-associated crystallins from aging and cataractous human lenses.
Invest Ophthalmol Vis Sci. 1987 May;28(5):780-4.
9
The effects of hyperbaric oxygen on the crystallins of cultured rabbit lenses: a possible catalytic role for copper.高压氧对培养兔晶状体晶状体蛋白的影响:铜的可能催化作用。
Exp Eye Res. 2000 Oct;71(4):371-83. doi: 10.1006/exer.2000.0887.
10
Increase in the intramolecular disulfide bonding of alpha-A crystallin during aging of the human lens.人晶状体老化过程中α-A晶状体蛋白分子内二硫键的增加。
Exp Eye Res. 1996 Nov;63(5):585-90. doi: 10.1006/exer.1996.0149.

引用本文的文献

1
New insights into the mechanisms of age-related protein-protein crosslinking in the human lens.关于人眼晶状体中与年龄相关的蛋白质-蛋白质交联机制的新见解。
Exp Eye Res. 2021 Aug;209:108679. doi: 10.1016/j.exer.2021.108679. Epub 2021 Jun 17.
2
Identification of a 70,000-D protein in lens membrane junctional domains.晶状体膜连接结构域中一种70,000道尔顿蛋白质的鉴定。
J Cell Biol. 1985 Jul;101(1):28-35. doi: 10.1083/jcb.101.1.28.