Purification of Pumpkin GlutathioneS-Transferase Species Specifically Present in Cultured Cells Treated by Excessive Concentration of 2,4-Dichlorophenoxyacetic Acid but Absent in Normal Plants | Zendy

Masayuki Fujita | Zendy; Yasuhiko Adachi | Zendy; Nobuo Sakato | Zendy

Open Access

Purification of Pumpkin GlutathioneS-Transferase Species Specifically Present in Cultured Cells Treated by Excessive Concentration of 2,4-Dichlorophenoxyacetic Acid but Absent in Normal Plants

Author(s) -

Masayuki Fujita,

Yasuhiko Adachi,

Nobuo Sakato

Publication year - 1998

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.62.2431

Subject(s) - glutathione , antiserum , glutathione s transferase , biochemistry , chemistry , protein subunit , affinity chromatography , transferase , 2,4 dichlorophenoxyacetic acid , enzyme , column chromatography , chromatography , biology , microbiology and biotechnology , antigen , botany , immunology , gene

Pugc is a unique glutathione S-transferase subunit species that is absent in normal pumpkin plants, but GST3c (homodimer of Pugc) accumulates in cultured pumpkin cells treated with 40 ppm 2,4-dichlorophenoxyacetic acid for six days. GST3c was purified by DEAE-cellulose, hydroxylapatite, and S-hexylglutathione-agarose column chromatography, and its homogeneity was confirmed by SDS-PAGE analysis. The specific activity of GST3c was 124 μmol/min/mg protein with 1-chloro-2,4-dinitrobenzene. This was higher than those of the other plant and animal glutathione S-transferases. Mouse antiserum raised against the purified GST3c recognized only Pugc, but not Puga, Pugb, nor Pugd when the reactivity of pumpkin glutathione S-transferase subunits was tested.

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