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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

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

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.[1]

References

  1. Identification of a highly reactive sulphydryl group in human placental glutathione transferase by a site-directed fluorescent reagent. Lo Bello, M., Petruzzelli, R., De Stefano, E., Tenedini, C., Barra, D., Federici, G. FEBS Lett. (1990) [Pubmed]
 
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