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PMID: 2192576 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

An alternative quenched fluorescence substrate for Pz-peptidase.

Analytical biochemistry ·Vol. 186 ·No. 1 ·1990-04-00 ·Pages 112-5

Tisljar U, Knight CG, Barrett AJ

Abstract

7-Methoxycoumarin-3-carboxylyl-Pro-Leu-Gly-Pro-D-Lys(2,4-dinitr oph enyl) is introduced as a new quenched fluorescence substrate for assaying Pz-peptidase (also known as soluble metallo-endopeptidase and endo-oligopeptidase). The value of Km for partially purified Pz-peptidase from rat muscle was 8.6 microM. High protein concentrations did not interfere with the assay, so that for the first time continuous assays of Pz-peptidase in crude tissue extracts became possible.

MeSH Terms
Amino Acid Sequence Chemical Phenomena Chemistry Endopeptidases/analysis Fluorescence Hydrolysis Kinetics Metalloendopeptidases Molecular Sequence Data Oligopeptides/metabolism Substrate Specificity
Chemicals
Oligopeptides 7-methoxycoumarin-3-carboxylyl-prolyl-leucyl-glycyl-prolyl-lysyl-2,4-dinitrophenyl Endopeptidases Metalloendopeptidases thimet oligopeptidase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Tisljar U
Biochemistry Department, Strangeways Research Laboratory, Cambridge, United Kingdom.
Knight C G
Barrett A J
Article Info
Journal
Analytical biochemistry
Abbr.
Anal Biochem
ISSN
0003-2697
Published
1990-04-00
Pages
112-5
Language
English
Region
United States
NLM ID
0370535
Subset
IM
Grants
Wellcome Trust · United Kingdom
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