Purification and characterization of lens specific calpain (Lp82) from bovine lens.

@article{Ueda2001PurificationAC,
  title={Purification and characterization of lens specific calpain (Lp82) from bovine lens.},
  author={Yoji Ueda and Ashley L. McCormack and Thomas Rodney Shearer and Larry Leroy David},
  journal={Experimental eye research},
  year={2001},
  volume={73 5},
  pages={
          625-37
        }
}
Ubiquitous type m-calpain and lens specific Lp82 calpain were separated and partially purified from fetal bovine lens and the enzymatic characteristics were compared. Lens m-calpain required 200 microM calcium for 1/2 maximal activity, while Lp82 required 30 microM. Both types of calpains were inhibited by 0.1 mM E64, and 5 mM iodoacetamide, but not by 1 mM phenylmethylsulfonyl fluoride. Lp82 was insensitive to 1 microM calpastatin peptide while m-calpain was effectively inhibited. In the… CONTINUE READING
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