title: N-Me-pAB-Glu-gamma-Glu-gamma-Tyr(3-NO(2)): an internally quenched fluorogenic gamma-glutamyl hydrolase substrate.
abstract: 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.
authors: Departments of Chemistry and Medicinal Chemistry, University of Michigan, Ann Arbor, MI 48109-1055, USA.
authors: J J
authors: JJ
authors: Pankuch
authors: J K
authors: JK
authors: Coward
mesh_terms: D000818:Animals; D002851:Chromatography, High Pressure Liquid; D005456:Fluorescent Dyes / Q000737:chemistry* / Q000493:pharmacokinetics*; D006868:Hydrolysis; D007700:Kinetics; D013058:Mass Spectrometry; D009842:Oligopeptides / Q000737:chemistry* / Q000493:pharmacokinetics*; D051381:Rats; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D013050:Spectrometry, Fluorescence; D013329:Structure-Activity Relationship; D011623:gamma-Glutamyl Hydrolase / Q000737:chemistry / Q000378:metabolism*
chemical_list: D005456:Fluorescent Dyes; C442979:N-Me-pAB-Glu-gamma-Glu-gamma-Tyr(3-NO(2)); D009842:Oligopeptides; D011994:Recombinant Proteins; D011623:gamma-Glutamyl Hydrolase