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pubmed-article:15820140pubmed:abstractTextA 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.lld:pubmed
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pubmed-article:15820140pubmed:authorpubmed-author:ChibaAkiraAlld:pubmed
pubmed-article:15820140pubmed:authorpubmed-author:SaitohEiichiElld:pubmed
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pubmed-article:15820140pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:15820140pubmed:year2005lld:pubmed
pubmed-article:15820140pubmed:articleTitleA novel cysteine protease inhibitor with lectin activity from the epidermis of the Japanese eel Anguilla japonica.lld:pubmed
pubmed-article:15820140pubmed:affiliationDepartment of Biochemistry, The Nippon Dental University School of Dentistry at Niigata, 1-8 Hamaura-cho, Niigata 951-8580, Japan. esaitoh@ngt.ndu.ac.jplld:pubmed
pubmed-article:15820140pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:15820140pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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