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pubmed-article:15249048pubmed:abstractTextThe lysozyme of the marine bivalve, Tapes japonica (13.8 kDa), belongs to the invertebrate lysozyme family and displays both chitinase and isopeptidase activities. We determined the complete cDNA sequence and constructed effective expression systems for this enzyme using Escherichia coli (BL21) and Pichia pastoris. The native and recombinant proteins indicated lysozyme activity and isopeptidase activity, including the proteolysis of d-dimer, a plasminolytic product of stabilized polymeric fibrin. These results will be utilized for the structural and functional study of invertebrate lysozymes, and for the development of applications for thrombosis therapies.lld:pubmed
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pubmed-article:15249048pubmed:authorpubmed-author:ThujihataYosh...lld:pubmed
pubmed-article:15249048pubmed:authorpubmed-author:IomotoTaijiTlld:pubmed
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pubmed-article:15249048pubmed:volume36lld:pubmed
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pubmed-article:15249048pubmed:pagination254-62lld:pubmed
pubmed-article:15249048pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:15249048pubmed:year2004lld:pubmed
pubmed-article:15249048pubmed:articleTitleDetermination of the complete cDNA sequence, construction of expression systems, and elucidation of fibrinolytic activity for Tapes japonica lysozyme.lld:pubmed
pubmed-article:15249048pubmed:affiliationGraduate School of Pharmaceutical Sciences, Kyushu University, Fukuoka 812-8582, Japan.lld:pubmed
pubmed-article:15249048pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:15249048pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed