期刊
JOURNAL OF PROTEOME RESEARCH
卷 6, 期 10, 页码 3935-3943出版社
AMER CHEMICAL SOC
DOI: 10.1021/pr070138h
关键词
post-translational modification; 2D LC-MS/MS; cataract; human lens; tryptophan; oxidation
资金
- NEI NIH HHS [R01EY013570-03] Funding Source: Medline
The urea-soluble proteins from the nucleus of two young, two aged, and two early-stage nuclear cataract lenses were subjected to tryptic digestion and analysis by 2D LC-MS/MS. Several novel post-translational modifications were identified. Deamidation was, by far, the most common modification. A number of differences were found in cataract compared to normal lenses, most notably an increase in the number of oxidized tryptophan residues. Semiquantitative analysis revealed that there appeared to be a trend toward increased levels of deamidation with age; however, there was no apparent increase upon the onset of nuclear cataract. This is in contrast to Trp oxidation, where an increase in the extent of modification was apparent in cataract lenses when compared to aged normal lenses. These findings suggest Trp oxidation may be involved in nuclear cataract development.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据