Field Desorption Mass Spectra of Gastrine Peptides and Glutathione Derivatives

Abstract

Oligopeptides comprising the sequence of the C-terminal tetrapeptide of gastrine, Trp-Met-Asp-Phe-NH2, and several derivatives of glutathione, γ-Glu-Cys(SR)-Gly, were characterized by field desorption mass spectrometry. The field desorption mass spectra obtained at various field ion emitter temperatures reveal abundant molecular ions and fragmentation reactions that yield partial sequence information. In the series of glutathione derivatives investigated, characteristic ions formed by cleavage of the γ-Glu-Cys peptide bond determine the substituent at the Cys residue and can therefore be used to identify corresponding conjugation products of drug metabolites with glutathione.