Time of flight versus ion trap MS coupled to CE to analyse intact proteins.
In this work, two different CE-MS instruments, namely, CE-ESI-IT-MS and CE-ESI-TOF-MS, applied to analyse intact proteins from complex samples are investigated. The aim of this work was to compare both instruments in terms of LOD, number of proteins detected, and precision and repeatability in the determination of the protein relative molecular mass. Results show that although CE-ESI-IT-MS provides cleaner MS spectra of intact proteins, CE-ESI-TOF-MS allows the identification of a higher number of proteins from complex matrices in an easier way. Performance in terms of peak area reproducibility, LOD and precision in the determination of the molecular mass were similar for both instruments. The usefulness of the optimised CE-ESI-IT-MS and CE-ESI-TOF-MS conditions was demonstrated by studying the zein-proteins composition of three natural maize lines and their corresponding transgenic lines, showing no significant differences.
Erny
Guillaume L
GL
Institute of Industrial Fermentations (CSIC), Madrid, Spain.
León
Carlos
C
Marina
Maria Luisa
ML
Cifuentes
Alejandro
A
D002623:Chemistry Techniques, Analytical / Q000379:methods; D019075:Electrophoresis, Capillary / Q000295:instrumentation / Q000379:methods*; D005504:Food Analysis / Q000379:methods; D013058:Mass Spectrometry / Q000295:instrumentation / Q000379:methods*; D010940:Plant Proteins / Q000032:analysis; D030821:Plants, Genetically Modified / Q000378:metabolism; D015203:Reproducibility of Results; D021241:Spectrometry, Mass, Electrospray Ionization / Q000295:instrumentation / Q000379:methods*; D013997:Time Factors; D003313:Zea mays / Q000235:genetics*
D010940:Plant Proteins