• Medicine
  • Published in FEBS letters 1993

Beta-crystallins insolubilized by calpain II in vitro contain cleavage sites similar to beta-crystallins insolubilized during cataract.

@article{David1993BetacrystallinsIB,
  title={Beta-crystallins insolubilized by calpain II in vitro contain cleavage sites similar to beta-crystallins insolubilized during cataract.},
  author={Larry L. David and Thomas R. Shearer},
  journal={FEBS letters},
  year={1993},
  volume={324 3},
  pages={
          265-70
        }
}
Incubation of soluble proteins from rat lens with the protease calpain II caused the precipitation of beta-crystallin polypeptides. Two-dimensional electrophoresis and sequence analysis identified beta-crystallin polypeptides both before and after their precipitation by calpain II. beta-crystallin polypeptides precipitated by calpain were cleaved at their NH2-terminal extensions. These cleavage sites were similar to cleavage sites occurring in beta-crystallin polypeptides precipitated during… CONTINUE READING

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