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Characterization of abnormal human haemoglobins by fast atom bombardment mass spectrometry
Author(s) -
Pucci P.,
Ferranti P.,
Marino G.,
Malorni A.
Publication year - 1989
Publication title -
biomedical and environmental mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 0887-6134
DOI - 10.1002/bms.1200180105
Subject(s) - edman degradation , fast atom bombardment , mass spectrometry , globin , peptide , chemistry , chromatography , peptide mapping , characterization (materials science) , protein mass spectrometry , peptide sequence , hemoglobin , tandem mass spectrometry , biochemistry , materials science , gene , nanotechnology
A procedure using fast atom bombardment mass spectrometry for mapping the proteolytic digest of α‐, β‐ and γ‐globin chains of normal human haemoglobin was developed. It required the separation of globins prior to their analysis by mass spectrometry of their enzymatic digests. Almost all the expected peptides were identified by direct analysis of the peptide mixture. Peptide recognition along the globin chain sequences was easily made on the basis of their molecular weight and the assignments performed were confirmed submitting the whole peptide mixture to a single step of Edman degradation. The procedure was successfully applied to the structural characterization of three variant human β‐globin chains, demonstrating the general applicability of this mapping procedure in the analysis of haemoglobinopathies.