ASIA unversity:Item 310904400/4437
English  |  正體中文  |  简体中文  |  全文笔数/总笔数 : 90120/105278 (86%)
造访人次 : 8950277      在线人数 : 65
RC Version 6.0 © Powered By DSPACE, MIT. Enhanced by NTU Library IR team.
搜寻范围 查询小技巧:
  • 您可在西文检索词汇前后加上"双引号",以获取较精准的检索结果
  • 若欲以作者姓名搜寻,建议至进阶搜寻限定作者字段,可获得较完整数据
  • 进阶搜寻


    题名: Cloning and expression of human haptoglobin subunits in Escherichia coli: delineation of a major antioxidant domain
    作者: Lai IH;Tsai TI;Lin HH;Lai WY;Mao SJT
    贡献者: Department of Biotechnology
    日期: 2007-04
    上传时间: 2009-11-26 09:43:09 (UTC+8)
    出版者: Asia University
    摘要: Human plasma haptoglobin (Hp) comprises alpha and beta subunits. The alpha subunit is heterogeneous in size, therefore isolation of Hp and its subunits is particularly difficult. Using Escherichia coli, we show that alpha1, alpha2, beta, and alpha2beta chain was abundantly expressed and primarily present in the inclusion bodies consisting of about 30% of the cell-lysate proteins. Each cloned subunit retained its immunoreactivity as confirmed using antibodies specific to alpha or beta chain. By circular dichroism, the structure of each expressed subunit was disordered as compared to the native Hp. The antioxidant activity was found to be associated with both alpha and beta chains when assessed by Cu(2+)-induced oxidation of low density lipoprotein (LDL). Of remarkable interest, the antioxidant activity of beta chain was extremely potent and markedly greater than that of native Hp (3.5x), alpha chain (10x) and probucol (15x). The latter is a clinically proved potent compound used for antioxidant therapy. The "unrestricted" structure of beta subunit may therefore render its availability for free-radical scavenge, which provides a utility for the future design of a "mini-Hp" in antioxidant therapy. It may also provide a new insight in understanding the mechanism involved in the antioxidant nature of Hp.
    關聯: Protein Expression and Purification 52(2):356-62
    显示于类别:[生物科技學系] 期刊論文


    档案 描述 大小格式浏览次数
    310904400-4437 .doc30KbMicrosoft Word226检视/开启


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