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A novel cysteine protease inhibitor with lectin activity from the epidermis of the Japanese eel Anguilla japonica.

Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology (2005-04-12)
Eiichi Saitoh, Satoko Isemura, Akira Chiba, Shunya Oka, Shoji Odani
RESUMEN

A novel cysteine protease inhibitor (Eel-CPI-1) was isolated from the epidermis of the eel. Eel-CPI-1 was shown to bind strongly to both lactose- and carboxymethylated papain-affinity gels. Its molecular mass under reducing condition was determined to be 18 kDa by SDS-polyacrylamide gel electrophoresis but approximately 30.5 kDa under non-reducing-conditions. Eel-CPI-1 inhibited papain (K(i)=18 nM) and ficin (K(i)=120 nM) competitively. Combined with the data on amino acid and sequence analysis, Eel-CPI-1 is identical to the eel lectin, AJL-2. This is the first report describing a cysteine protease inhibitor with lectin activity.

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Sigma-Aldrich
Ficin from fig tree latex, lyophilized powder
Sigma-Aldrich
Ficin from fig tree latex, powder, ≥0.1 unit/mg solid
Sigma-Aldrich
Ficin from fig tree latex, saline suspension, ≥1.0 units/mg protein (biuret)