Purification and Properties of Soluble and Bound γ-Glutamyltransferases from Radish Cotyledon

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Soluble and cell wall bound γ-glutamyltransferases (GGTs) were purified from radish (<I>Raphanus sativus</I> L.) cotyledons. Soluble GGTs (GGT I and II) had the same <I>M</I><SUB>r</SUB> of 63,000, and were composed of a heavy subunit (<I>M</I><SUB>r</SUB>, 42,000) and a light one (<I>M</I><SUB>r</SUB>, 21,000). The properties of GGT I and II were similar. Bound GGTs (GGT A and B) were purified to homogeneity from the pellet after the extraction of soluble GGTs. GGT A and B were monomeric proteins with an <I>M</I><SUB>r</SUB> of 61,000. The properties of GGT A and B were similar. Thus, bound GGTs were distinguished from soluble GGTs. The optimal pHs of soluble and bound GGTs were about 7.5. Both soluble and bound GGTs utilized glutathione, γ-<small>L</small>-glutamyl-<I>p</I>-nitroanilide, oxidized glutathione and the conjugate of glutathione with monobromobimane as substrates, and were inhibited by acivicin, but soluble GGTs were also distinguished from bound GGTs with regard to these properties.

収録刊行物

  • Bioscience, biotechnology, and biochemistry  

    Bioscience, biotechnology, and biochemistry 70(2), 369-376, 2006-02-23 

    Japan Society for Bioscience, Biotechnology, and Agrochemistry

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各種コード

  • NII論文ID(NAID)
    10018534073
  • 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
    7833404
  • 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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