Molecules 2004, 9(6), 427-439; doi:10.3390/90600427
Article

The Preparation of Fluorescence-Quenched Probes for Use in the Characterization of Human Factor Xa Substrate Binding Domains

Received: 4 March 2004; Accepted: 14 March 2004 / Published: 31 May 2004
(This article belongs to the Special Issue RACI 2003 symposium)
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Abstract: The preparation and characterization by LCMS of a library of 55 fluorescence- quenched peptides is described. The peptides bear a terminal anthranilamide fluorophore and a penultimate 2,4-dinitrophenyl-L-lysine quencher, and will be used to probe the substrate binding domain of the human blood coagulation enzyme, factor Xa.
Keywords: Solid phase peptide synthesis; parallel synthesis; fluorescence-quenched substrates; protease; factor Xa.
PDF Full-text Download PDF Full-Text [212 KB, uploaded 18 June 2014 19:26 CEST]

Export to BibTeX |
EndNote


MDPI and ACS Style

Bromfield, K.M.; Cianci, J.; Duggan, P.J. The Preparation of Fluorescence-Quenched Probes for Use in the Characterization of Human Factor Xa Substrate Binding Domains. Molecules 2004, 9, 427-439.

AMA Style

Bromfield KM, Cianci J, Duggan PJ. The Preparation of Fluorescence-Quenched Probes for Use in the Characterization of Human Factor Xa Substrate Binding Domains. Molecules. 2004; 9(6):427-439.

Chicago/Turabian Style

Bromfield, Karen M.; Cianci, Julia; Duggan, Peter J. 2004. "The Preparation of Fluorescence-Quenched Probes for Use in the Characterization of Human Factor Xa Substrate Binding Domains." Molecules 9, no. 6: 427-439.

Molecules EISSN 1420-3049 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert