Date of Award
7-1-2019
Thesis Type
masters
Document Type
Thesis (Restricted Access)
Divisions
science
Department
Institute of Biological Sciences
Institution
Universiti Malaya
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.
Note
Dissertation (M.A.) – Faculty of Science, Universiti Malaya, 2019.
Recommended Citation
Christina Kong, Wen Hui, "Purification and partial characterization of glutathione s-transferases from Pseudomonas sp. UW4 / Christina Kong Wen Hui" (2019). Student Works (2010-2019). 6491.
https://knova.um.edu.my/student_works_2010s/6491