BIOINFORMATIC ANALYSIS AND PURIFICATION OF GLUTATHIONE TRANSFERASE (GST) from Pseudomonas sp. UW4
نویسندگان
چکیده
The study aimed at identifying and purifying cytosolic glutathione transferase isoforms expressed in Pseudomonas sp. UW4. Search UniProt (https://www.uniprot.org/uniprot/), has indicated that there were 20 genes encoding putative transferases for the microorganism. molecular weights of ranged from 17.6 to 34.06 kDa. SDS-polyacrylamide gel electrophoresis revealed GST purified using Sulfobromophthalein-glutathione (BSP) affinity column, resolved into a single band with low weight (MW) 16 kDa pI value 6.0. Purified was reactive towards ethacrynic acid, 1-chloro-2,4-dinitrobenzene, cumene hydroxide, hydrogen peroxide, but no detectable activity Trans-2-octenal, hepta-2,4-dienal Trans-4-phenyl-3-butene-2-one. This proven possessed peroxidase proposed be similar PputUW4_00801 (putative S-transferase) UW4 according its estimated values obtained experimentally.
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ژورنال
عنوان ژورنال: Malaysian applied biology
سال: 2022
ISSN: ['0126-8643', '2462-151X']
DOI: https://doi.org/10.55230/mabjournal.v51i4.27