期刊
EXPERIMENTAL EYE RESEARCH
卷 71, 期 2, 页码 195-207出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1006/exer.2000.0868
关键词
human lens; mass spectrometry; cataract; water-insoluble crystallins
资金
- NEI NIH HHS [EY RO1 07609] Funding Source: Medline
This investigation of the water-insoluble crystallins from human lenses has used multiple chromatographic separations to obtain proteins of sufficient purity for mass spectrometric analysis. Each fraction was analysed to determine the molecular masses of the constituent proteins as well as peptides in tryptic digests of these proteins. The major components of the water-insoluble crystallins were identified as alpha A-and alpha B-crystallins. In addition, gamma S-, beta B1-, gamma D-, beta A3/A1- and beta B2-crystallins were found, in order of decreasing abundance. Although there was evidence of some backbone cleavage, the predominant forms of alpha A-, alpha B, beta B2-, gamma S- and gamma D-crystallins were the intact polypeptide chains, The major modifications distinguishing the water-soluble crystallins were increased disulfide bonding, oxidation of Met, deamidation of Gin and Asn and backbone cleavage, Of the many reactions hypothesized to lead to crystallin insolubility and cataract, these results most strongly support metal-catalysed oxidation, deamidation and truncation as initiators of conformational changes that Favor aggregation. (C) 2000 Academic Press.
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