English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

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.

bioscience, biotechnology, and biochemistry

Purification of Pumpkin Glutathione<i>S</i>-Transferase Species Specifically Present in Cultured Cells Treated by Excessive Concentration of 2,4-Dichlorophenoxyacetic Acid but Absent in Normal Plants

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