ArticlePlant physiology1998
Isolation and characterization of glutathione S-transferase isozymes from sorghum.
Article in Plant physiology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- Hematological and Biochemical Alterations Induced by Sub-Acute Administration of Permethrin in Rats.Journal of xenobiotics · 2025Article
- Study of Glutathione S-Transferase, Its Isoenzyme (Pi), and Tumor Markers (CA15-3, HE4) in Breast Carcinoma Patients (Before and After Treatment).Journal of pharmacy & bioallied sciences · 2025Review
- Analysis of Essential Isoprene Metabolic Pathway Proteins inApplied and environmental microbiology · 2023Article
- Article
- Differential Response of Phenol Metabolism Associated with Antioxidative Network in Elicited Grapevine Suspension Cultured Cells under Saline Conditions.Antioxidants (Basel, Switzerland) · 2022Article
- Exogenous 3,3'-Diindolylmethane Improves Vanadium Stress Tolerance inBiomolecules · 2021Article
- Mechanism of Resistance toFrontiers in plant science · 2021Article
- Lipid Peroxide-Derived Reactive Carbonyl Species as Mediators of Oxidative Stress and Signaling.Frontiers in plant science · 2021Review
- Combined effects of cadmium and oil sludge on sorghum: growth, physiology, and contaminant removal.Environmental science and pollution research international · 2020Article
- Plant growth promotingHeliyon · 2020Article
- Yeast glutaredoxin, GRX4, functions as a glutathione S-transferase required for red ade pigment formation inJournal of biosciences · 2020Article
- Reactive Carbonyl Species: A Missing Link in ROS Signaling.Plants (Basel, Switzerland) · 2019Review
- Purification and characterization of glutathione S-transferase from blueberry fruits (Heliyon · 2019Article
- Redox-regulated methionine oxidation of Arabidopsis thaliana glutathione transferase Phi9 induces H-site flexibility.Protein science : a publication of the Protein Society · 2019Article
- Transcriptome Profiling and Genome-Wide Association Studies RevealFrontiers in plant science · 2019Article
- Detoxification of Reactive Carbonyl Species by Glutathione Transferase Tau Isozymes.Frontiers in plant science · 2019Article
- Functional, Structural and Biochemical Features of Plant Serinyl-Glutathione Transferases.Frontiers in plant science · 2019Review
- Biochemical characterization of metabolism-based atrazine resistance in Amaranthus tuberculatus and identification of an expressed GST associated with resistance.Plant biotechnology journal · 2017Article
- Insights into ligand binding to a glutathione S-transferase from mango: Structure, thermodynamics and kinetics.Biochimie · 2017Article
- Article
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2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two glutathione S-transferase (GST) isozymes, A1/A1 and B1/B2, were purified from etiolated, O-1,3-dioxolan-2-yl-methyl-2,2,2, -trifluoro-4'-chloroacetophenone-oxime-treated sorghum (Sorghum bicolor L. Moench) shoots. GST A1/A1, a constitutively expressed homodimer, had a subunit molecular mass of 26 kD and an isoelectric point of 4.9. GST A1/A1 exhibited high activity with 1-chloro-2, 4, dinitrobenzene (CDNB) but low activity with the chloroacetanilide herbicide metolachlor. For GST A1/A1, the random, rapid-equilibrium bireactant kinetic model provided a good description of the kinetic data for the substrates CDNB and glutathione (GSH). GST B1/B2 was a heterodimer with subunit molecular masses of 26 kD (designated the B1 subunit) and 28 kD (designated the B2 subunit) and a native isoelectric point of 4.8. GST B1/B2 exhibited low activity with CDNB and high activity with metolachlor as the substrate. The kinetics of GST B1/B2 activity with GSH and metolachlor fit a model describing a multisite enzyme having two binding sites with different affinities for these substrates. Both GST A1/A1 and GST B1/B2 exhibited GSH-conjugating activity with ethacrynic acid and GSH peroxidase activity with cumene hydroperoxide, 9-hydroperoxy-trans-10, cis-12-octadecadienoic acid and 13-hydroperoxy-cis-9, trans-11-octadecadienoic acid. Both GST A1/A1 and GST B1/B2 are glycoproteins, as indicated by their binding of concanavalin A. Polyclonal antibodies raised against GST A1/A1 exhibited cross-reactivity with the B1 subunit of GST B1/B2. Comparisons of the N-terminal amino acid sequences of the GST A1, B1, and B2 subunits with other type I theta-GSTs indicated a high degree of homology with the maize GST I subunit and a sugarcane GST.
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