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.
Full text not available from this repository.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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