文摘
The coupling of Fourier transform ion cyclotron resonancemass spectrometry (FTICR MS) with electrospray ionization has advanced the analysis of large biopolymers andprovided the basis for high-throughput protein characterization (e.g., for rapid "proteome" analyses). In thiswork, the combination of high-performance capillaryliquid chromatography with FTICR mass spectrometryand external ion accumulation has been shown to increaseboth sensitivity and analysis duty cycle. Instrument versatility is further improved by ion preselection followedby ion accumulation in an external linear quadrupole iontrap. The interface was tested with a 3.5-T FTICR massspectrometer and evaluated with a number of peptidesand proteins whose molecular weights ranged from 500to 66 000. A significant increase in the sensitivity, dutycycle, and dynamic range over that of the previously usedaccumulated trapping was achieved, exhibiting a detectionlimit of ~10 zmol (~6000 molecules) for smaller proteinssuch as cytochrome c. Capillary LC external accumulationinterface with FTICR was successfully applied for thestudy of whole-proteome mouse tryptic digests.