Camel brain glutathione S-transferase purification, properties, regional and subcellular distribution.
1. Camel brain glutathione S-transferase was purified by glutathione-linked agarose affinity column and the different isozymes were separated by chromatofocusing. 2. The basic isozymes which comprise 45% of the total activity were immunologically indistinguishable from the near-neutral isozymes which constitute 55% of the activity. 3. Some differences were detectable among the basic and near-neutral isozymes in relation to substrate specificities and subunit composition. 4. Biochemical and immunological quantification of glutathione S-transferase revealed the presence of the enzyme in all camel brain regions tested and subcellular fractions. 5. The pons had the highest concentration of the enzyme and the cortex had the lowest, while more than 88% of the enzyme was present in the cytosol.
Hunaiti
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Department of Biological Sciences, Yarmouk University, Irbid, Jordan.
Asa'd
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D000818:Animals; D001921:Brain / Q000201:enzymology* / Q000648:ultrastructure; D002162:Camelus / Q000378:metabolism*; D002845:Chromatography; D003600:Cytosol / Q000201:enzymology; D004137:Dinitrochlorobenzene / Q000378:metabolism; D004355:Drug Stability; D004591:Electrophoresis, Polyacrylamide Gel; D005982:Glutathione Transferase / Q000032:analysis* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D005779:Immunodiffusion; D007122:Immunoelectrophoresis; D007526:Isoelectric Point; D007527:Isoenzymes / Q000032:analysis* / Q000378:metabolism; D008970:Molecular Weight; D011149:Pons / Q000201:enzymology; D013379:Substrate Specificity; D014018:Tissue Distribution
D004137:Dinitrochlorobenzene; D007527:Isoenzymes; D005982:Glutathione Transferase