Subcellular Localization and Possible Functions of γ-Glutamyltransferase in the Radish (Raphanus sativus L.) Plant

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Author(s)

Abstract

Previously we reported the purification of soluble γ-glutamyltransferases (GGTs) from radish cotyledon. Subcellular fractionation of radish cells revealed that soluble GGT is a vacuolar enzyme. Acivicin, a GGT inhibitor, mediated the <I>in vivo</I> catabolism inhibition of the glutathione <I>S</I>-conjugate generated from endogenous glutathione and exogenously supplied monochlorobimane. Thus soluble GGT is possibly involved in the catabolism of glutathione <I>S</I>-conjugates.

Journal

  • Bioscience, Biotechnology, and Biochemistry

    Bioscience, Biotechnology, and Biochemistry 70(7), 1790-1793, 2006-07-23

    Japan Society for Bioscience, Biotechnology, and Agrochemistry

References:  23

Cited by:  2

Codes

  • NII Article ID (NAID)
    10018529627
  • NII NACSIS-CAT ID (NCID)
    AA10824164
  • Text Lang
    ENG
  • Article Type
    Journal Article
  • ISSN
    09168451
  • NDL Article ID
    7998241
  • NDL Source Classification
    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 Call No.
    Z53-G223
  • Data Source
    CJP  CJPref  NDL  J-STAGE 
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