Hemoglobin NYU, a delta chain variant, α2δ212Lys

Helen M. Ranney; Alan S. Jacobs; Bracha Ramot; Thomas B. Bradley

doi:10.1172/JCI106171

Hemoglobin NYU, a delta chain variant, α₂δ₂^12Lys

Published November 1, 1969 - More info

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Abstract

A minor hemoglobin (Hb) component with the electrophoretic properties of the δ-chain variant Hb A_2′ 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 A_2′ 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.

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