Purification and characterization of cathepsin D from the lizard Agama stellio stellio

الملخص EN

Cathepsin D was isolated from the lizard Agama stellio stellio skeletal muscle and purified to electrophoretical homogeneity for the first time in lizards species by concanavalin A-sepharose and sephadex G-100 chromatographies Purified cathepsin D from skeletal muscle of this lizard appeared to be electrophoretically homogenous and had a molecular weight of 6400 Daltons estimated by sephadex G-100 and 67000 Daltons by SDS-PAGE.

This enzyme was completely inhibited by.

Pepstatin, Hg2+, and Fe3+ and was partially inhibited by phenyl methyl sulfonyl florid (PMSF) P-chloromercuribenzoate (PCMB).

SDS, and iodoacetic acid.

(IAA).

The PI of this enzyme was 5.13, and the optimal pH and temperature were 3.5 and 37ْ C respectively.