Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10820572 | Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology | 2005 | 7 Pages |
Abstract
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 (Ki = 18 nM) and ficin (Ki = 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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Authors
Eiichi Saitoh, Satoko Isemura, Akira Chiba, Shunya Oka, Shoji Odani,