Mass measurements of C-terminally truncated alpha-crystallins from two-dimensional gels identify Lp82 as a major endopeptidase in rat lens.

Molecular & cellular proteomics : MCP

Volumn 1, Issue 5, 2002, Pages 357-365

  Ueda, Yoji ^a   Fukiage, Chiho ^a   Shih, Marjorie ^a   Shearer, Thomas R ^a   David, Larry L ^a  

^a OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CRYSTALLIN; CALCIUM; CALPAIN; CALPAIN 3; ISOPROTEIN; M CALPAIN; M-CALPAIN;

ANIMAL; ARTICLE; CELL NUCLEUS; CHEMISTRY; DOSE RESPONSE; ENZYMOLOGY; LENS; MASS SPECTROMETRY; METABOLISM; MOLECULAR CLONING; PROTEIN PROCESSING; PROTEIN TERTIARY STRUCTURE; RAT; SPRAGUE DAWLEY RAT; TIME; TWO DIMENSIONAL GEL ELECTROPHORESIS;

ALPHA-CRYSTALLINS; ANIMALS; CALCIUM; CALPAIN; CELL NUCLEUS; CLONING, MOLECULAR; DOSE-RESPONSE RELATIONSHIP, DRUG; ELECTROPHORESIS, GEL, TWO-DIMENSIONAL; LENS, CRYSTALLINE; MASS SPECTROMETRY; PROTEIN ISOFORMS; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, TERTIARY; RATS; RATS, SPRAGUE-DAWLEY; TIME FACTORS;

EID: 0036582510     PISSN: 15359476     EISSN: None     Source Type: Journal    
DOI: 10.1074/mcp.M200007-MCP200     Document Type: Article

References (0)