Electrophoretic separation of sickle-cell hemoglobins in 1949 introduced the concept of "molecular diseases." Since then, electrophoretic techniques have been perfected to separate, identify, and quantitate other normal and abnormal hemoglobins. The simple approach of electrophoresis makes it possible to diagnose the chief inherited disorders of hemoglobin, including sickle cell disease and the thalassemias.
A molecule of human hemoglobin contains two pairs of polypeptide chains, each composed of more than 140 amino acid residues.1 Fetal hemoglobin (F) consists of one pair of alpha and one pair of gamma chains, whereas adult hemoglobin (A) consists of pairs of alpha and beta chains. Hemoglobin A2, which is generally 2.5% of the hemoglobin in the adult, consists of alpha and delta chains. The alpha chains in the three varieties of normal hemoglobin are identical, but there are multiple differences in the amino acid sequences of the gamma, beta, and delta chains. The abnormalities
Louderback AL, Shanbrom E. Hemoglobin Electrophoresis. JAMA. 1967;202(8):718–719. doi:10.1001/jama.1967.03130210092016
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