English  |  正體中文  |  简体中文  |  Items with full text/Total items : 54367/62174 (87%)
Visitors : 12961108      Online Users : 81
RC Version 6.0 © Powered By DSPACE, MIT. Enhanced by NTHU Library IR team.
Scope Tips:
  • please add "double quotation mark" for query phrases to get precise results
  • please goto advance search for comprehansive author search
  • Adv. Search
    HomeLoginUploadHelpAboutAdminister Goto mobile version
    National Tsing Hua University Institutional Repository > 生命科學院  > 生命科學系 > 期刊論文 >  Heparin binding stabilizes the membrane-bound form of cobra cardiotoxin


    Please use this identifier to cite or link to this item: http://nthur.lib.nthu.edu.tw/dspace/handle/987654321/48414


    Title: Heparin binding stabilizes the membrane-bound form of cobra cardiotoxin
    Authors: Shih-Che Sue;Kun-Yi Chien;Wei-Ning Huang;Joseph K. Abraham;Kuan-Ming Chen;Wen-guey Wu
    教師: 吳文桂
    Date: 2002
    Publisher: American Society for Biochemistry and Molecular Biology
    Relation: JOURNAL OF BIOLOGICAL CHEMISTRY,American Society for Biochemistry and Molecular Biology,Volume 277,Issue 4,JAN 25 2002,Pages 2666-2673
    Keywords: PHOSPHOLIPASE A(1)
    CRYSTAL-STRUCTURE
    SPECTROSCOPY
    Abstract: It has been shown previously that the long chain fragments of heparin bind to the beta-strand cationic belt of the three-finger cobra cardiotoxin (or cytotoxin, CTX) and hence enhance its penetration into phospholipid monolayer under physiological ionic conditions. By taking lysophosphatidyleholine (LPC) micelles as a membrane model, we have shown by H-1 NAIR study that the binding of heparin-derived hexasaccharide (Hep-6) to CTX at the beta-strand region can induce conformational changes of CTX near its membrane binding loops and promote the binding activity of CTX toward LPC. The Fourier-transform infrared spectra and NAIR nuclear Overhauser effect of Hep-6(.)CTX and (CTXLPC)-L-. complex in aqueous buffer also supplemented the aforementioned observation. Thus, the detected conformational change may presumably be the result of structural coupling between the connecting loops and its P-strands. This is the first documentation of results showing how the association of hydrophilic carbohydrate molecules with amphiphilic proteins can promote hydrophobic protein-lipid interaction via the stabilization of its membrane-bound form. A similar mechanism involving tripartite interactions of heparin, protein, and lipid molecules may be operative near the extracellular matrix of cell membranes.
    URI: http://www.asbmb.org/
    http://nthur.lib.nthu.edu.tw/dspace/handle/987654321/48414
    Appears in Collections:[生命科學系] 期刊論文

    Files in This Item:

    File Description SizeFormat
    index.html0KbHTML355View/Open


    在NTHUR中所有的資料項目都受到原著作權保護,僅提供學術研究及教育使用,敬請尊重著作權人之權益。若須利用於商業或營利,請先取得著作權人授權。
    若發現本網站收錄之內容有侵害著作權人權益之情事,請權利人通知本網站管理者(smluo@lib.nthu.edu.tw),管理者將立即採取移除該內容等補救措施。

    SFX Query

    與系統管理員聯絡

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