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  • Title: Purification of rat liver plasma membrane glutathione transferase.
    Author: Horbach ME, Sies H, Akerboom TP.
    Journal: Eur J Biochem; 1994 May 15; 222(1):91-6. PubMed ID: 8200358.
    Abstract:
    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.
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