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標題: Characterisation of 2-Cys peroxiredoxin isozyme (Prx1) from Taiwanofungus camphorata (Niu-chang-chih): Expression and enzyme properties
作者: Liau, Y.J.
Chen, Y.T.
Lin, C.Y.
Huang, J.K.
Lin, C.T.
關鍵字: Taiwanofungus camphorata;Three-dimensional homology structure (3-D;homology structure);2-Cys peroxiredoxin isozyme (Prx1);parasite plasmodium-falciparum;alkyl hydroperoxide reductase;antrodia-camphorata;hydrogen-peroxide;biochemical-characterization;superoxide-dismutase;1-cys peroxiredoxin;antioxidant;catalase;thioredoxin
Project: Food Chemistry
期刊/報告no:: Food Chemistry, Volume 119, Issue 1, Page(s) 154-160.
Peroxiredoxins (Prxs) are a family of antioxidant peroxidases. The functions of Prxs comprises of cell protection against oxidative stress and regulation of cell proliferation. A putative 2-Cys Prx isozyme (Prx1) cDNA was cloned from Taiwanofungus camphorata (commonly known as Niu-chang-chih in Taiwan). The deduced amino acid sequence is conserved amongst the reported Prxs. A 3-D homology structure was created for this Prx1. To characterise the T camphorata Prx1, the coding region was subcloned into a pAVD10 and transformed into Escherichia coli. The recombinant 6His-tagged Prx1 was expressed and purified by Ni(2+)-nitrilotriacetic acid sepharose. The purified enzyme showed two forms using a 15% SDS-PAGE. The enzyme retained 60% activity at 60 degrees C for 2.5 min. The enzyme was stable under a broad pH range from 5 to 11. The enzyme showed 57% activity after 40 min of incubation at 37 degrees C with trypsin. The ability of the enzyme to protect intact supercoiled plasmid DNA from (center dot)OH induced nicking was demonstrated. (C) 2009 Elsevier Ltd. All rights reserved.
ISSN: 0308-8146
DOI: 10.1016/j.foodchem.2009.06.008
Appears in Collections:基因體暨生物資訊學研究所

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