A single intact red blood cell (erythrocyte) was injected into a capillary electrophoresis column, and following in-capillary lysing the alpha- and beta-chains of the hemoglobin (approximately 450 amol) were separated and detected using capillary electrophoresis/electrospray ionization time-of-flight mass spectrometry. The mass specta of the electropherogram peaks of the alpha and beta chains showed identifiable peaks corresponding to multiply protonated and sodiated alpha- and beta-chains of hemoglobin.