Saitoh Eiichi, Isemura Satoko, Chiba Akira, Oka Shunya, Odani Shoji
Department of Biochemistry, The Nippon Dental University School of Dentistry at Niigata, 1-8 Hamaura-cho, Niigata 951-8580, Japan.
Comp Biochem Physiol B Biochem Mol Biol. 2005 May;141(1):103-9. doi: 10.1016/j.cbpc.2005.02.002.
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.