Christina Kong , Wen Hui (2019) Purification and partial characterization of glutathione s-transferases from Pseudomonas sp. UW4 / Christina Kong Wen Hui. Masters thesis, Universiti Malaya.
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Abstract
Glutathione transferases (GSTs) obtained from University of Waterloo, Canada, were purified from Pseudomonas sp. UW4, by glutathione-affinity chromatography, identified through bioinformatic analysis and their substrate specificities were investigated. SDS-polyacrylamide gel electrophoresis revealed that the GST purified using Sulfobromophthalein-glutahione (BSP) affinity column resolved into a single band with low molecular weight (MW) of 17 kDa. Isoselectrofocusing showed it exists in single band with pI value of 6.1. 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 demonstrated that putative GST possessed peroxidase activity but is not involved in lipid peroxidation. The purified GST suggested to be similar to PputUW4_00801 (putative glutathione S-transferase) of Pseudomonas sp. UW4.
| Item Type: | Thesis (Masters) |
|---|---|
| Additional Information: | Dissertation (M.A.) – Faculty of Science, Universiti Malaya, 2019. |
| Uncontrolled Keywords: | Purification; Glutathione-s-transferase; Sulfobromophthalein-glutahione; Affinity column; Pseudomonas sp. UW4 |
| Subjects: | Q Science > Q Science (General) Q Science > QA Mathematics |
| Divisions: | Faculty of Science |
| Depositing User: | Mr Mohd Safri Tahir |
| Date Deposited: | 09 Oct 2024 01:55 |
| Last Modified: | 09 Oct 2024 01:55 |
| URI: | http://studentsrepo.um.edu.my/id/eprint/15143 |
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