Secondary ion mass spectra of tryptic peptides of human hemoglobin chains

Secondary ion mass spectra of tryptic peptides of human globin alpha-, beta-, gamma and delta-chains were studied. Almost all mass peaks of protonated molecular ions of tryptic peptides were observed and they were very stable and abundant. The present results show the possibilities for quantitative analysis of two gamma-globin species: A gamma and G gamma chains, and for structural analysis of unknown abnormal hemoglobins.