Abstract
Glutathione S-transferase P (GST-P) bound a series of endogenous fatty acids (C 12-C 18). To clarify the function and the binding site of the fatty acids, interaction between fatty acids and GST-P was investigated by using 12- (9-anthroyloxy) stearic acid conjugated with Woodward's reagent K. The fluorescence-conjugated fatty acid noncompetitively inhibited GST activity. After GST-P was covalently labeled with the fatty acid, the enzyme was digested with Lysyl Endopeptidase. From the peptide mapping, a single fluorescence-labeled peptide was obtained. By the sequence analysis, the peptide binding fatty acid was determined as the residues of 141–188 from the amino terminus.
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