rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
12
|
pubmed:dateCreated |
2001-6-19
|
pubmed:abstractText |
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.
|
pubmed:grant |
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jun
|
pubmed:issn |
0960-894X
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
18
|
pubmed:volume |
11
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1561-4
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:11412981-Animals,
pubmed-meshheading:11412981-Chromatography, High Pressure Liquid,
pubmed-meshheading:11412981-Fluorescent Dyes,
pubmed-meshheading:11412981-Hydrolysis,
pubmed-meshheading:11412981-Kinetics,
pubmed-meshheading:11412981-Mass Spectrometry,
pubmed-meshheading:11412981-Oligopeptides,
pubmed-meshheading:11412981-Rats,
pubmed-meshheading:11412981-Recombinant Proteins,
pubmed-meshheading:11412981-Spectrometry, Fluorescence,
pubmed-meshheading:11412981-Structure-Activity Relationship,
pubmed-meshheading:11412981-gamma-Glutamyl Hydrolase
|
pubmed:year |
2001
|
pubmed:articleTitle |
N-Me-pAB-Glu-gamma-Glu-gamma-Tyr(3-NO(2)): an internally quenched fluorogenic gamma-glutamyl hydrolase substrate.
|
pubmed:affiliation |
Departments of Chemistry and Medicinal Chemistry, University of Michigan, Ann Arbor, MI 48109-1055, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|