ABSTRACT
Fast heavy ions, i.e. fission fragments from a 252Cf-source, have been used to desorb and ionize peptides and proteins from a sample surface. Masses of the desorbed ions have been determined by the time-of-flight technique. The mass interval of the molecules studied is 1000-14 000 u. Quasi-molecular ions of higher masses than earlier reported have been observed. The results include the detection of quasi-molecular ions of proinsulins, cytochrome-C, ribonuclease and two phospholipases. The general features of mass spectra of proteins using this ionization method are described. Emphasis is put on the discussion of metastable ion decay, neutral components, multiply charged ions, isotopic broadening, and cluster ion formation. Also the precision which can be obtained with a straight time-of-flight mass spectrometer will be discussed. Future applications of the technique are outlined.
