Statements in which the resource exists as a subject.
PredicateObject
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: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.