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pubmed-article:16091588pubmed:abstractTextThe lectin from Agrocybe aegerita (AAL) has been found to possess potent tumor-suppressing function and tumor cell apoptosis-inducing activity. In this paper, we report the full sequence, the active expression of the gene encoding AAL at a high level and bioassay of the binding property with lactose, apoptosis-inducing activity and DNase activity of recombinant AAL (rAAL). The results reveal that AAL is a member of the galectin family and the dimeric form is the active unit for the functional performance. The rAAL showed comparable tumor cell apoptosis-inducing activity with the wild AAL but no DNase activity at all. The molecular characters revealed by this study are significant for the in-depth investigation of the functional mechanism of this interesting protein.lld:pubmed
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pubmed-article:16091588pubmed:authorpubmed-author:ZhangYingYlld:pubmed
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pubmed-article:16091588pubmed:dateRevised2007-12-19lld:pubmed
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pubmed-article:16091588pubmed:year2005lld:pubmed
pubmed-article:16091588pubmed:articleTitleMolecular character of the recombinant antitumor lectin from the edible mushroom Agrocybe aegerita.lld:pubmed
pubmed-article:16091588pubmed:affiliationCenter for Structural and Molecular Biology, Institute of Biophysics, Chinese Academy of Science, Beijing.lld:pubmed
pubmed-article:16091588pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:16091588pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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