The abnormal haemoglobins in haemoglobin-H disease

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Abstract
The hemolysates from four individuals with Hb-H disease were examined and each contained three abnormal hemoglobins without enchains, namely Bh-[beta]a4, Hb-[gamma]f4 and Hb-[delta]A2. These three hemoglobins have been isolated, characterized by electrophoresis in starch gel and starch block, peptide mapping, ultraviolet- and visible-absorption spectra and alkaline denaturation rate. Hb-[beta]A4 gives a peptide map identical with that of the BA-chains of normal nb-A. Its tryptophan fine-structure band is an unresolved inflexion in the adult position, and is alkaline denaturation rate is fast and comparable with that of Hb-A. Hb-[gamma]f4 gives a peptide map identical with that of the [gamma] F- chains of normal Hb-F. Its tryptophan fine-structure band is in the fetal position, but is resolved to a greater degree than in Hb-F. It is relatively resistant to alkaline denaturation, but its behavior in this respect is not identical with Hb-F. Hb-[delta]A2 gives a peptide map identical with that of the 5a2-chains of Hb-A2. Its tryptophan fine-structure band is an unresolved inflexion in the adult position, and its alkaline denaturation rate is fast and of the same order as the rates for Hb-A and Hb-A2. The proportions of Hb-[beta]A4, Hb-[gamma]f4 and Hb-[delta]A2 vary in the four cases studied. The findings are discussed in relation to present concepts of the final stages of normal hemoglobin synthesis and their disturbance in Hb-H disease.