Kinetic analysis of the cleavage of human protease-activated receptor-1/2/3 and 4 using quenched-fluorescent peptide substrates

Mark Fox, Brett Greer, Jill Lawson, Adrienne Healy, Patrick Harriott

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Protease-activated receptors [PARs] are a family of G-protein-coupled seven-transmembrane domain receptors that are activated by proteolytic cleavage of their amino-terminal exodomain. To characterize the cleavage rate of human PAR-1 / 2 / 3 and 4 by trypsin and thrombin, four synthetic quenched-fluorescent peptide substrates have been synthesized. Each substrate consisted of a ten-residue peptide spanning the receptor activation cleavage site and using progress-curve kinetics, k(cat)/K-m values were determined.
Original languageEnglish
Pages (from-to)387-393
Number of pages7
JournalProtein and Peptide Letters
Volume9
Issue number5
Publication statusPublished - 2002

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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