Cytosolic glutathione transferases (GSTs) were purified from the rat spleen by S-hexyl-GSH-Sepharose chromatography, and two major forms were identified as GSTs 2-2 and 7-7 (GST P). Besides these forms an acidic form (pI 5.8) was purified by chromatofocusing at pH 7-4 and it accounted for about 1% of the total GST activity bound to S-hexyl-GSH-Sepharose. Two-dimensional gel electrophoresis revealed that it is a homodimer (subunit Mr 26,000 with pI 5.8). Immunoblot analysis demonstrated that it was immunologically related to GSTs 2-2 and 1-1, and its N-terminal amino acid was apparently blocked, similarly to other forms of the class Alpha. This form had a low activity towards cumene hydroperoxide or 4-hydroxynon-2-enal, indicating that this form differed from GSTs 10-10 and 8-8 as well as from GSTs 1-1 and 2-2. These results suggest that it is a new form of GST belonging to the class Alpha.
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March 1990
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Research Article|
March 01 1990
Rat spleen glutathione transferases. A new acidic form belonging to the Alpha class
S Tsuchida;
S Tsuchida
1Second Department of Biochemistry, Hirosaki University School of Medicine, Zaifu-cho 5, Hirosaki 036, Japan
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K Sato
K Sato
1Second Department of Biochemistry, Hirosaki University School of Medicine, Zaifu-cho 5, Hirosaki 036, Japan
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Publisher: Portland Press Ltd
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© 1990 London: The Biochemical Society
1990
Biochem J (1990) 266 (2): 461–465.
Citation
S Tsuchida, K Sato; Rat spleen glutathione transferases. A new acidic form belonging to the Alpha class. Biochem J 1 March 1990; 266 (2): 461–465. doi: https://doi.org/10.1042/bj2660461
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