National Taiwan Ocean University Institutional Repository:Item 987654321/27019
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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/27019

Title: Characterisation of 2-Cys peroxiredoxin isozyme (Prx1) from Taiwanofungus camphorata (Niu-chang-chih): Expression and enzyme properties
Authors: Yi-Jen Liau;Yu-Ting Chen;Choa-Yi Lin;Jenq-Kuen Huang;Chi-Tsai Lin
Contributors: NTOU:Institute of Bioscience and Biotechnology
國立臺灣海洋大學:生物科技研究所
Keywords: Taiwanofungus camphorata;Three-dimensional homology structure (3-D homology structure);2-Cys peroxiredoxin isozyme (Prx1)
Date: 2010-03-01
Issue Date: 2011-10-21T02:22:20Z
Publisher: Food Chemistry
Abstract: Abstract: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 Ni2+-nitrilotriacetic acid sepharose. The purified enzyme showed two forms using a 15% SDS–PAGE. The enzyme retained 60% activity at 60 °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 °C with trypsin. The ability of the enzyme to protect intact supercoiled plasmid DNA from ·OH induced nicking was demonstrated.
Relation: 119(1), pp.154–160
URI: http://ntour.ntou.edu.tw/handle/987654321/27019
Appears in Collections:[Department of Bioscience and Biotechnology ] Periodical Articles

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