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      Identification of a highly reactive sulphydryl group in human placental glutathione transferase by a site-directed fluorescent reagent.

      Febs Letters
      Amino Acid Sequence, Chromatography, High Pressure Liquid, Fluorescent Dyes, Glutathione Transferase, metabolism, Humans, Maleimides, Molecular Sequence Data, Peptide Fragments, analysis, Placenta, enzymology, Sulfhydryl Compounds

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          Abstract

          A fluorescent maleimide derivative, N-(4-anilino-1-naphthyl) maleimide (ANM), a specific probe for thiol groups, reacted with human placental glutathione transferase (GST, EC 2.5.1.18), causing a complete inactivation of the enzyme in a few minutes. The modified enzyme was denatured, alkylated and digested with (L-1-tosylamide-2-phenylethyl chloromethyl ketone)-trypsin. The tryptic digest was analysed by HPLC and a fluorescent peptide was obtained. The sequence of this peptide allowed us, by a comparison with a well known primary structure, to assign the position 47 to the most reactive cysteine of GST enzyme.

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