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Differentiation of Electrophoretically Similar Hemoglobins—Such as S, D, G, and P; or A2, C, E, and O—by Electrophoresis of the Globin Chains
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1974
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Electrophoretically Similar Hemoglobins—suchGlycobiologyMolecular BiologyMolecular GeneticsAnalytical UltracentrifugationRedox BiologyHeme TraffickingBioanalysisHematologyAnalytical ChemistryIsotachophoresisBiophysicsChromatographyCapillary ElectrophoresisBiochemistryCellulose AcetateMolecular ChargeHeme TransportBiomedical AnalysisHeme HomeostasisGlobin ChainsNatural SciencesHeme DegradationAlkaline BuffersElectrophysiologyO—by ElectrophoresisMedicine
Abstract Electrophoresis of the globin chains of hemoglobin on cellulose acetate in both acidic and alkaline buffers (pH about 6 and 9) containing urea and 2-mercaptoethanol is a simple, rapid means of characterizing hemoglobins. Erythrocyte hemolysate is electrophoresed in the presence of a large amount of mercaptoethanol, which liberates heme from globin, and keeps it in solution during its rapid electrophoretic removal. Each globin chain migrates at a characteristic rate, which varies with the pH and composition of the buffer. The combined data permit differentiation, with a high degree of specificity, of some similarly charged hemoglobins. They may also be useful in assessing the effect of secondary and tertiary structure on molecular charge.