Protein fingerprint by fast atom bombardment mass spectrometry: Characterization of normal and variant human haemoglobins

Abstract

A procedure using fast atom bombardment mass spectrometry was developed for mapping the proteolytic digest of proteins. The procedure was successfully applied to the tryptic peptides of the human β-globin chain. Almost all the expected peptides were identified by direct analysis of the peptide mixture on the mass spectrometer. Peptide recognition along the β-globin chain sequence was easily made on the basis of their molecular weight. The general applicability of this mapping procedure in the analysis of haemoglobinopathies was demonstrated by its use for the structural characterization of a variant β-globin chain.