Analysis of high-mass biomolecules using electrostatic fields and matrix-assisted laser desorption/ionization in a Fourier transform mass spectrometer.

A new decelerating technique that places dc potentials on the orthogonal excitation and receiver plates as well as the rear trapping plate (conductance limit) of the source cell of a dual cubic cell has been applied to the standard matrix-assisted laser desorption/ionization Fourier transform mass spectrometry technique. When this five-plate trapping method is applied, high-mass ions with large translational kinetic energies can be trapped efficiently and detected. Using this approach, low-resolution spectra of carbonic anhydrase (MW = 29,000), egg albumin (MW = 45,000), and bovine albumin (MW = 66,000) have been obtained. Because the new decelerating method requires no modification to the existing cell, it is also possible to obtain high-resolution spectra for compounds with masses of ca. 14,000 Da and lower. Utilizing the five-plate trapping method, a bovine insulin spectrum with a resolving power of 20,000 was obtained. It is not yet possible to obtain higher resolution for the higher mass proteins. The reasons for this difficulty are currently being investigated.