The major in vivo modifications of the human water-insoluble lens crystallins are disulfide bonds, deamidation, methionine oxidation and backbone cleavage

Experimental Eye Research

Volumn 71, Issue 2, 2000, Pages 195-207

  Hanson, Stacy R A ^a   Hasan, Azeem ^a   Smith, David L ^a   Smith, Jean B ^a  

^a UNIVERSITY OF NEBRASKA LINCOLN   (United States)

Author keywords

Cataract; Human lens; Mass spectrometry; Water insoluble crystallins

Indexed keywords

CRYSTALLIN; LENS PROTEIN; METHIONINE;

ARTICLE; CATARACT; DISULFIDE BOND; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HUMAN; HUMAN TISSUE; LENS; MOLECULAR WEIGHT; PRIORITY JOURNAL; PROTEIN ANALYSIS;

EID: 0033829222     PISSN: 00144835     EISSN: None     Source Type: Journal    
DOI: 10.1006/exer.2000.0868     Document Type: Article

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