Glutathione S-transferases of human brain
نویسندگان
چکیده
Human brain contains one cationic (pI8.3) and two anionic (pI5.5 and 4.6) forms of glutathione S-transferase. The cationic form (pI 8.3) and the less-anionic form (p1 5.5) do not correspond to any of the glutathione S-transferases previously characterized in human tissues. Both of these forms are dimers of 26 500-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 (pl 4.6) is a dimer of 24 500-Mr and 22 500Mr subunits. Two-dimensional gel electrophoresis demonstrates that there are three types of 26 500-Mr subunits, two types of 24 500-Mr subunits and two types of 22 500Mr subunits present in the glutathione S-transferases of human brain.
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