Separation of hemoglobin variants by ion-exchange chromatography on Monobead resins.
Our studies on the separation of hemoglobin variants using Monobead ion exchangers show that these ion exchangers will resolve variants that heretofore could not be resolved. Procedures with these ion exchangers, therefore, extend our ability to detect hemoglobinopathies. Since it is also important to study the physicochemical properties of variants, their isolation is of critical importance to the researcher. The methods described in this report enable variants to be isolated in quantitative amounts so that such studies can be performed. Most isolations can be accomplished within 1 h, under mild conditions with aqueous buffers. Elution gradients can be changed conveniently to optimize resolution of most variants. These methods should serve as a valuable adjunct in studying the structure-function relationship of hemoglobin and other proteins.
D002852:Chromatography, Ion Exchange / Q000379:methods; D005312:Fetal Blood / Q000032:analysis; D006441:Hemoglobin A / Q000032:analysis; D006451:Hemoglobin, Sickle / Q000032:analysis; D006454:Hemoglobins / Q000032:analysis*; D006801:Humans; D007231:Infant, Newborn
D006451:Hemoglobin, Sickle; D006454:Hemoglobins; D006441:Hemoglobin A