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

Abstract

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… (More)

Topics

Cite this paper

@article{Ueda2001PurificationAC, title={Purification and characterization of lens specific calpain (Lp82) from bovine lens.}, author={Yosimichi Ueda and Ashley L. McCormack and Thomas R. Shearer and Larry David}, journal={Experimental eye research}, year={2001}, volume={73 5}, pages={625-37} }