Analysis of High-Mass Biomolecules Using Electrostatic Fields and Matrix-Assisted Laser Desorption/Ionization in a Fourier Transform Mass Spectrometer

Publisher Website
Google Scholar
Abstract
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.

This publication has 0 references indexed in Scilit: