Purification, Characterization, and Sequencing of Novel Antimicrobial Peptides, Tu-AMP 1 and Tu-AMP 2, from Bulbs of Tulip (Tulipa gesneriana L.)

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Novel antimicrobial peptides (AMP), designated <I>Tu</I>-AMP 1 and <I>Tu</I>-AMP 2, were purified from the bulbs of tulip (<I>Tulipa gesneriana</I> L.) by chitin affinity chromatography and reverse-phase high-performance liquid chromatography (HPLC). They bind to chitin in a reversible way. They were basic peptides having isoelectric points of over 12. <I>Tu</I>-AMP 1 and <I>Tu</I>-AMP 2 had molecular masses of 4,988 Da and 5,006 Da on MALDI-TOF MS analysis, and their extinction coefficients of 1% aqueous solutions at 280 nm were 3.3 and 3.4, respectively. Half of all amino acid residues of <I>Tu</I>-AMP 1 and <I>Tu</I>-AMP 2 were occupied by cysteine, arginine, lysine, and proline. The concentrations of peptides required for 50% inhibition (IC<SUB>50</SUB>) of the growth of plant pathogenic bacteria and fungi were 2 to 20 μg/ml. The structural characteristics of <I>Tu</I>-AMP 1 and <I>Tu</I>-AMP 2 indicated that they were novel thionin-like antimicrobial peptides, though <I>Tu</I>-AMP 2 was a heterodimer composes of two short peptides joined with disulfide bonds.

収録刊行物

  • Bioscience, biotechnology, and biochemistry

    Bioscience, biotechnology, and biochemistry 68(3), 571-577, 2004-03-23

    公益社団法人 日本農芸化学会

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各種コード

  • NII論文ID(NAID)
    10013142753
  • NII書誌ID(NCID)
    AA10824164
  • 本文言語コード
    ENG
  • 資料種別
    ART
  • ISSN
    09168451
  • NDL 記事登録ID
    6904232
  • NDL 雑誌分類
    ZR7(科学技術--農林水産--農産) // ZR2(科学技術--生物学--生化学) // ZP1(科学技術--化学・化学工業)
  • NDL 請求記号
    Z53-G223
  • データ提供元
    CJP書誌  CJP引用  NDL  J-STAGE 
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