
A gamma-glutamyl tripeptide containing an internally quenched fluorophore has been synthesized and shown to be a substrate for recombinant rat gamma-glutamyl hydrolase. HPLC, LC-MS, and fluorescence spectra support the conclusion that selective hydrolysis occurs at the penultimate peptide bond. Preliminary data indicate that hydrolysis of this substrate can be monitored continuously to yield steady-state kinetic data.
Hydrolysis, gamma-Glutamyl Hydrolase, Mass Spectrometry, Recombinant Proteins, Rats, Kinetics, Structure-Activity Relationship, Spectrometry, Fluorescence, Animals, Oligopeptides, Chromatography, High Pressure Liquid, Fluorescent Dyes
Hydrolysis, gamma-Glutamyl Hydrolase, Mass Spectrometry, Recombinant Proteins, Rats, Kinetics, Structure-Activity Relationship, Spectrometry, Fluorescence, Animals, Oligopeptides, Chromatography, High Pressure Liquid, Fluorescent Dyes
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