Purification of rat liver plasma membrane glutathione transferase.
Glutathione transferases purified from plasma membrane and microsomal fractions from rat liver share similar enzymic properties. The activity of both proteins with 1-chloro-2,4-dinitrobenzene can be stimulated about 10-15-fold by N-ethylmaleimide. No activation is observed using p-nitrobenzylchloride as a substrate. The enzymes are immunologically related as indicated by Western-blot analysis using antibodies against the microsomal glutathione transferase or against a synthetic peptide corresponding to the amino acid positions 55-64 of microsomal glutathione transferase. Isolated plasma membrane and microsomal glutathione transferases possess the same amino-terminal amino acid sequence and digestion with different proteases results in identical fragment patterns as displayed by SDS/PAGE. These data suggest that plasma membrane and microsomal glutathione transferase are identical proteins.
Horbach
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ME
Institut für Physiologische Chemie I, Heinrich-Heine-Universität Düsseldorf, Germany.
Sies
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H
Akerboom
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TP
D000595:Amino Acid Sequence; D000818:Animals; D015153:Blotting, Western; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D005982:Glutathione Transferase / Q000302:isolation & purification* / Q000378:metabolism; D007425:Intracellular Membranes / Q000201:enzymology; D008862:Microsomes, Liver / Q000201:enzymology*; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D051381:Rats; D013379:Substrate Specificity
D005982:Glutathione Transferase