Analysis of soluble proteins from Campylobacter jejuni by matrix-assisted laser desorption/ionization-time of flight mass spectrometry

This study was carried out to establish a proteome analysis of Campylobacter jejuni (C. jejuni). The proteins of C. jejuni lysate were separated by two-dimensional gel electrophoresis (2-DE) and stained with silver nitrate. The each protein spot on the 2-DE gel was digested with trypsin and analyzed by peptide mass fingerprinting (PMF) using matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOFMS). Approximately 400 spots were observed on a silver-stained gel using a pH 4～7 immobilized pH gradient (IPG) strip. Approximately 150 spots from the gel were chosen for PMF analysis. Thirty two of them were identified successfully as Campylobacter jejuni. This result might provide a strategy for identifying Campylobacter jejuni proteins using proteome analysis.