Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
|
pubmed:dateCreated |
1992-3-27
|
pubmed:abstractText |
(7-methoxycoumarin-4-yl)Acetyl-Pro-Leu-Gly-Leu-(3-[2,4-dinitrophenyl]-L- 2,3-diaminopropionyl)-Ala-Arg-NH2 (Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2) has been synthesised as a fluorogenic substrate for the matrix metalloproteinases. The highly fluorescent 7-methoxycoumarin group is efficiently quenched by energy transfer to the 2,4-dinitrophenyl group. The punctuated metalloproteinase (PUMP, EC 3.4.24.23) cleaves the substrate at the Gly-Leu bond with a 190-fold increase in fluorescence (lambda cx 328 nm, lambda cm 393 nm). In assays of the human matrix metalloproteinases. Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 is about 50 to 100 times more sensitive than dinitrophenyl-Pro-Leu-Gly-Leu-Trp-Ala-D-Arg-NH2 and continuous assays can be made at enzyme concentrations comparable to those used with macromolecular substrates. Specificity constants (kcat/Km) are reported for both synthetic substrates with PUMP, collagenase, stromelysin and 72 kDa gelatinase.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Jan
|
pubmed:issn |
0014-5793
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
27
|
pubmed:volume |
296
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
263-6
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:1537400-Amino Acid Sequence,
pubmed-meshheading:1537400-Chromatography, High Pressure Liquid,
pubmed-meshheading:1537400-Coumarins,
pubmed-meshheading:1537400-Extracellular Matrix,
pubmed-meshheading:1537400-Humans,
pubmed-meshheading:1537400-Metalloendopeptidases,
pubmed-meshheading:1537400-Molecular Sequence Data,
pubmed-meshheading:1537400-Oligopeptides,
pubmed-meshheading:1537400-Sensitivity and Specificity,
pubmed-meshheading:1537400-Substrate Specificity
|
pubmed:year |
1992
|
pubmed:articleTitle |
A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteinases.
|
pubmed:affiliation |
Strangeways Research Laboratory, Worts Causeway, Cambridge, UK.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|