Human brain contains one cationic (pI8.3) and two anionic (pI5.5 and 4.6) forms of glutathione S-transferase. The cationic form (pI8.3) and the less-anionic form (pI5.5) do not correspond to any of the glutathione S-transferases previously characterized in human tissues. Both of these forms are dimers of 26500-Mr subunits; however, immunological and catalytic properties indicate that these two enzyme forms are different from each other. The cationic form (pI8.3) cross-reacts with antibodies raised against cationic glutathione S-transferases of human liver, whereas the anionic form (pI5.5) does not. Additionally, only the cationic form expresses glutathione peroxidase activity. The other anionic form (pI4.6) is a dimer of 24500-Mr and 22500-Mr subunits. Two-dimensional gel electrophoresis demonstrates that there are three types of 26500-Mr subunits, two types of 24500-Mr subunits and two types of 22500-Mr subunits present in the glutathione S-transferases of human brain.
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January 1985
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Research Article|
January 15 1985
Glutathione S-transferases of human brain. Evidence for two immunologically distinct types of 26500-Mr subunits
Publisher: Portland Press Ltd
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© 1985 London: The Biochemical Society
1985
Biochem J (1985) 225 (2): 375–382.
Citation
C Theodore, S V Singh, T D Hong, Y C Awasthi; Glutathione S-transferases of human brain. Evidence for two immunologically distinct types of 26500-Mr subunits. Biochem J 15 January 1985; 225 (2): 375–382. doi: https://doi.org/10.1042/bj2250375
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