High-performance liquid chromatography analysis of N-acyl homoserine lactone hydrolysis by paraoxonases.

John F. Teiber, Dragomir I. Draganov

Research output: Contribution to journalArticle

7 Scopus citations

Abstract

Mammalian paraoxonases (PONs) are a unique, highly conserved family of calcium-dependent esterases consisting of PON1, PON2, and PON3. The PONs can hydrolyze the lactone ring of a range of N-acyl-L: -homoserine lactone (AHL) quorum sensing signaling molecules, rendering them inactive. This chapter describes a method that utilizes high-performance liquid chromatography analysis with UV detection for determining the rate of AHL hydrolysis in cell lysates, tissue homogenates, serum, and with purified proteins. Also described are the techniques used to prepare cell culture lysates and tissue homogenates for analysis and the use of class-specific enzyme inhibitors to determine the contribution of PONs to AHL hydrolysis in the samples.

Original languageEnglish (US)
Pages (from-to)291-298
Number of pages8
JournalMethods in molecular biology (Clifton, N.J.)
Volume692
DOIs
StatePublished - 2011

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

Fingerprint Dive into the research topics of 'High-performance liquid chromatography analysis of N-acyl homoserine lactone hydrolysis by paraoxonases.'. Together they form a unique fingerprint.

  • Cite this