English  |  正體中文  |  简体中文  |  全文筆數/總筆數 : 18240/20438 (89%)
造訪人次 : 5600070      線上人數 : 929
RC Version 7.0 © Powered By DSPACE, MIT. Enhanced by NTU Library IR team.
搜尋範圍 查詢小技巧:
  • 您可在西文檢索詞彙前後加上"雙引號",以獲取較精準的檢索結果
  • 若欲以作者姓名搜尋,建議至進階搜尋限定作者欄位,可獲得較完整資料
  • 進階搜尋
    請使用永久網址來引用或連結此文件: https://ir.cnu.edu.tw/handle/310902800/27096


    標題: ONE LECTIN ISOLATED FROM Croton tiglium
    Croton tiglium中一種植物凝集素的分離
    作者: Chen, Chin-Ching
    Fuh, Lih-Fang
    貢獻者: 私立嘉南藥學專科學校
    日期: 1981
    上傳時間: 2013-11-12 13:50:13 (UTC+8)
    摘要: A plant agglutinin was isolated and purified from Croton tiglium beans by DEAE- sephadex and gel – filtration chromatographies. The agglutinin had a molecular weight of 220,000 and was named Croton tiglium agglutinin 220 (CTA220). It had specific affinity to rabbit erythrocytes. However, it did not agglutinate pig erythrocytes. CTA220 was inhibited by L-fucose whereas RCA120, RCA60 (Ricinus communis agglutinins of molecular weights 120,000 and 60,000 respectively) and APA134 (Abrus precatorius agglutinin with molecular weight 134,000) were inhibited by galactose. Like RCA120, RCA60 and APA134 CTA220 had no hemolytic activity.
    經由DEAE- sephadex及gel – filtration柱層層析法,而從Croton tiglium 中分離出一種植物凝集素。此凝集素分子量為220,000,故簡稱為CTA220。
    CTA220對紅血球絕無溶血作用,而對兔子紅血球有強烈凝集作用,然對豬的紅血球則無此凝集反應。
    CTA220的凝集作用可被L-fucose抑制。
    關聯: 嘉南學報7, pp.29-36
    顯示於類別:[嘉南學報] 7期 (1981)

    文件中的檔案:

    沒有與此文件相關的檔案.



    在CNU IR中所有的資料項目都受到原著作權保護.

    TAIR相關文章

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