Purification of Pumpkin Glutathione S-Transferase Species Specifically Present in Cultured Cells Treated by Excessive Concentration of 2,4-Dichlorophenoxyacetic Acid but Absent in Normal Plants
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概要
- 論文の詳細を見る
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 124μmol/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 Puge, but not Puga, Pugb, nor Pugd when the reactivity of pumpkin glutathione S-transferase subunits was tested.
- 社団法人日本農芸化学会の論文
- 1998-12-23
著者
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FUJITA MASAYUKI
Department of Pathology, Kobe Medical Center
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Adachi Yasuhiko
Department Of Plant Sciences Faculty Of Agriculture Kagawa University
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SAKATO Nobuo
Department of Plant Sciences, Faculty of Agriculture, Kagawa University
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Fujita Masayuki
Department Of Plant Sciences Faculty Of Agriculture Kagawa University
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Sakato N
Ehime Univ. Ehime Jpn
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Fujita Masayuki
Department Of Applied Biological Science Laboratory Of Plant Stress Responses Faculty Of Agriculture
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Sakato Nobuo
Department of Life Sciences, Faculty of Agriculture, Kagawa University
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Fujita Masayuki
Department of Plant Sciences, Faculty of Agriculture, Kagawa University
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