Hemoglobin NYU, a delta chain variant, α2δ212Lys

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Abstract
A minor hemoglobin (Hb) component with the electrophoretic properties of the δ-chain variant Hb A2′ was encountered in two unrelated families of Russian-Jewish ancestry. This minor component, designated Hb NYU, was shown to result from the substitution of lysine for asparagine at δ12. We have confirmed studies of others that hemoglobin A2′ isolated from the hemoglobin of some African subjects, results from the replacement of the normal glycine at δ16 by arginine. Thus for interpretations of the incidence of δ-chain variants in different populations, electrophoretic data are not sufficient. In members of one of the families in the present study, the visual estimations of normal Hb A2 and of Hb NYU on starch-gel electrophoretic patterns suggested the presence of δ-thalassemia. In hemolysates of one of the heterozygotes for Hb NYU, hemoglobin A2 was not demonstrable with starch-gel electrophoretic methods but was readily recovered by column chromatography in approximately the amounts expected for δ-chain heterozygotes.