Bioinformatic analysis and purification of glutathione transferase (GST) from Pseudomonas sp. UW4

Kong, Christina Wen Hui and Tan, Irene Kit Ping and Zazali, Alias (2022) Bioinformatic analysis and purification of glutathione transferase (GST) from Pseudomonas sp. UW4. Malaysian Applied Biology, 51 (4). 177 – 184. ISSN 0126-8643, DOI https://doi.org/10.55230/mabjournal.v51i4.27.

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Abstract

The study aimed at identifying and purifying cytosolic glutathione transferase isoforms expressed in Pseudomonas sp. UW4. Search at UniProt (https://www.uniprot.org/uniprot/), has indicated that there were 20 genes encoding putative glutathione transferases for the microorganism. The molecular weights of the isoforms ranged from 17.6 to 34.06 kDa. SDS-polyacrylamide gel electrophoresis revealed that the GST purified using Sulfobromophthalein-glutathione (BSP) affinity column, resolved into a single band with a low molecular weight (MW) of 16 kDa with the pI value of 6.0. Purified GST was reactive towards ethacrynic acid, 1-chloro-2,4-dinitrobenzene, cumene hydroxide, and hydrogen peroxide, but no detectable activity with Trans-2-octenal, hepta-2,4-dienal and Trans-4-phenyl-3-butene-2-one. This has proven that putative GST possessed peroxidase activity and proposed to be similar to PputUW4₀₀₈₀₁ (putative glutathione S-transferase) of Pseudomonas sp. UW4 according to its estimated molecular weight and the pI values obtained experimentally. © 2022, Malaysian Society of Applied Biology. All rights reserved.

Item Type: Article
Funders: Kementerian Sains, Teknologi dan Inovasi [Grant no. FP034-2008C], Universiti Malaya [Grant no. PG176-2015A]
Uncontrolled Keywords: Affinity chromatography; glutathione transferases; Pseudomonas sp. UW4
Subjects: Q Science > QH Natural history > QH301 Biology
Divisions: Faculty of Science > Institute of Biological Sciences
Depositing User: Ms. Juhaida Abd Rahim
Date Deposited: 28 May 2025 01:55
Last Modified: 28 May 2025 01:55
URI: http://eprints.um.edu.my/id/eprint/43838

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