National Changhua University of Education Institutional Repository : Item 987654321/16778
English  |  正體中文  |  简体中文  |  全文筆數/總筆數 : 6507/11669
造訪人次 : 29932472      線上人數 : 426
RC Version 3.2 © Powered By DSPACE, MIT. Enhanced by NTU Library IR team.
搜尋範圍 進階搜尋

請使用永久網址來引用或連結此文件: http://ir.ncue.edu.tw/ir/handle/987654321/16778

題名: An Enzyme Possessing Both Glutathione-dependent Formaldehyde Dehydrogenase and S-nitrosoglutathione Reductase from Antrodia Camphorate
作者: Huang, Chih-Yu;Ken, Chuian-Fu;Wen, Lisa;Lin, Chi-Tsai
貢獻者: 生物學系
關鍵詞: Antrodia camphorata;Glutathione-dependent formaldehyde dehydrogenase (GFD or GSH-FDH);S-hydroxymethylglutathione (HMGSH);S-nitrosoglutathione (GSNO);S-nitrosoglutathione reductase (GSNOR)
日期: 2009-02
上傳時間: 2013-06-05T08:48:20Z
出版者: Elsevier
摘要: Glutathione-dependent formaldehyde dehydrogenase (GFD or GSH-FDH) plays important roles in formaldehyde detoxification and antioxidation. A gene encoding GFD from Antrodia camphorata was identified based on sequence homology. The deduced amino acid sequence of 378 amino acid residues is conserved among the reported GFDs. To characterise the Ac-GFD, the coding region was subcloned into a vector pET-20b(+) and transformed into Escherichia coli. The recombinant GFD was expressed and purified by Ni2+-nitrilotriacetic acid Sepharose. This purified enzyme showed a single band on a 10% SDS–PAGE. The enzyme retained 50% GFD activity after heating at 50 °C for 5 min. The enzyme is bifunctional. In addition to the GFD activity, it also functions as an effective S-nitrosoglutathione reductase (GSNOR) presumably to safeguard against nitrosative stress. The Km values for S-hydroxymethylglutathione and S-nitrosoglutathione were 1.20 and 0.28 mM, respectively.
關聯: Food Chemistry, 112(4): 795-802
顯示於類別:[生物學系] 期刊論文

文件中的檔案:

檔案 大小格式瀏覽次數
index.html0KbHTML629檢視/開啟


在NCUEIR中所有的資料項目都受到原著作權保護.

 

DSpace Software Copyright © 2002-2004  MIT &  Hewlett-Packard  /   Enhanced by   NTU Library IR team Copyright ©   - 回饋