Abstract
Multiple forms of glutathione S-transferase (EC 2.5.1.18), a family of proteins involved both with bilirubin transport and with the detoxification of electrophiles, have been purified from human liver using a scheme which employs an affinity chromatography column prepared by coupling glutathione to epoxy-activated Sepharose. This procedure offers a convenient method for obtaining highly purified transferases in good yields.
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