Structural analysis of human hemoglobin variants with field desorption mass spectrometry.
Tryptic hydrolyzates of normal and abnormal human globin chains were analyzed with mass spectrometry, using field desorption ionization technique. All the peptides, including core peptides, were detected as protonated molecular ions in field desorption mass spectra. Since the technique makes it possible to determine the mass number of each peptide, it is very useful for structural analysis of human hemoglobin variants, even those with electrophoretically and chromatographically silent mutations.
D000328:Adult; D055598:Chemical Phenomena; D002621:Chemistry; D005260:Female; D005312:Fetal Blood; D005914:Globins; D006441:Hemoglobin A; D006449:Hemoglobin M; D006451:Hemoglobin, Sickle / Q000235:genetics; D006455:Hemoglobins, Abnormal / Q000235:genetics; D006801:Humans; D007231:Infant, Newborn; D013058:Mass Spectrometry; D009154:Mutation; D010446:Peptide Fragments; D011247:Pregnancy; D014357:Trypsin
D006451:Hemoglobin, Sickle; D006455:Hemoglobins, Abnormal; D010446:Peptide Fragments; C027541:hemoglobin M Boston; D005914:Globins; D006441:Hemoglobin A; C029606:hemoglobin Genova; D006449:Hemoglobin M; D014357:Trypsin