Abstract
Incubation of soluble proteins from rat lens with the protease calpain II caused the precipitation of β-crystallin polypeptides. Two-dimensional electrophoresis and sequence analysis identified β-crystallin polypeptides both before and after their precipitation by calpain II. β-crystallin polypeptides precipitated by calpain were cleaved at their NH2-terminal extensions. These cleavage sites were similar to cleavage sites occurring in β-crystallin polypeptides precipitated during formation of experimental cataract induced by an overdose of selenite. These data suggested that calpain II caused β-crystallin insolubilization during cataract formation, and indicated that the process can be mimicked in vitro.
Original language | English (US) |
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Pages (from-to) | 265-270 |
Number of pages | 6 |
Journal | FEBS Letters |
Volume | 324 |
Issue number | 3 |
DOIs | |
State | Published - Jun 21 1993 |
Keywords
- Calpain
- Cataract
- Crystallin
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology