Abstract：Glutathione transferases (GST; EC2.5.1.18) is an important detoxification enzyme which catalyze the conjugation of glutathione to a large variety of endogenous and exogenous electrophilic compounds to protect the functions of body. In the present paper, three dimensional fluorescence spectra were obtained, through which the authors could identify the fluorescence spectra of peptide bond, Tyr and Trp residue. The authors compared aromatic amino-acid residue fluorescence spectra in GST with dissociative to know red or blue shift of the fluorescence peak. The authors also studied the peptide bond and Trp residue fluorescence spectra at various pH, which suggested the change in GST surface and surface hydrophobicity, and the microenviroment change of aromatic amino-acid residue in enzyme.
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