Micro‐high‐performance liquid chromatography/Fourier transform mass spectrometry with electron‐capture dissociation for the analysis of protein enzymatic digests

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Abstract

Abstract Electron‐capture dissociation (ECD) Fourier transform mass spectrometry (FTMS) employed to generate comprehensive sequence information for the chromatographic analysis of enzymatic protein digests is described. A pepsin digest of cytochrome c was separated by reversed‐phase micro‐high‐performance liquid chromatography (µHPLC) and ionized ‘on‐line’ by electrospray ionization (ESI). The ions thus formed were transferred to and trapped in the FTMS analyzer cell. Typically, no precursor ion isolation was performed. The trapped ions were subjected to a pulse of electrons to induce fragmentation. Mass spectra were acquired continuously to produce a three‐dimensional LC/MS data set. The spectra were dominated by c and, to a lesser degree, z ions, which provided near complete sequence coverage. External calibration provided good mass accuracy and resolution, typical of FTMS. Thus µHPLC/ECD − FTMS is shown to be a highly informative method for the analysis of enzymatic protein digests. Copyright © 2002 John Wiley & Sons, Ltd.

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