Micellar electrokinetic chromatography for analyzing active site specificity of Pseudomonas aeruginosa elastase

Simona Viglio, Giuseppe Zanaboni, Anna Lupi, Luca Gianelli, Maurizio Luisetti, Lucio Casali, Giuseppe Cetta, Paolo Iadarola

Research output: Contribution to journalArticlepeer-review

Abstract

The geometry of the catalytic site of Pseudomonas aeruginosa elastase was reexamined, exploiting the specific feature of micellar electrokinetic chromatography (MEKC), i.e., its ability to detect a decrease of intact substrate and simultaneous formation of reaction products. We carried out a detailed investigation using two tri- and six tetra-peptide 4-nitroanilides (NA) differing from each other by only one or more amine acids as stable substrates. The kinetic cleavage parameters K(m) and k(cat) determined by MEKC and the catalytic efficiency K(m)/k(cat) values calculated allowed us to better define the substrate specificity of this proteinase.

Original languageEnglish
Pages (from-to)1578-1585
Number of pages8
JournalElectrophoresis
Volume20
Issue number7
DOIs
Publication statusPublished - 1999

Keywords

  • Micellar electrokinetic chromatography
  • Protease active site

ASJC Scopus subject areas

  • Clinical Biochemistry

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