Abstract
MOST structural variants of human haemoglobin occur in smaller amounts than HbA in the peripheral blood of heterozygous subjects. Abnormal haemoglobins with mutations in the β chain usually comprise 35–45% of the haemoglobin in haemolysates. In contrast, haemoglobins with abnormal α chains generally amount to only 20–25% of the total haemoglobin. This difference in the proportion of α and β chain variants is thought to reflect the fact that in some populations there are two α loci and only one out of four α globin genes is affected in a heterozygote, whereas one out of two β globin alleles is abnormal in a subject with a β varient1,2. Certain unstable haemoglobins with critical alterations in β-chain structure also constitute a much smaller proportion of the total circulating haemoglobin than HbA. The low concentration of these abnormal haemoglobins is the result of accelerated preferential destruction3–7. We report here a new unstable β variant, Hb Bushwick, which was detected in an intact form constituting only 1–2% of the total circulating haemoglobin. Evidence was found for rapid postsynthetic destruction of the abnormal β chain. In spite of this accelerated loss of the product of one of the two β alleles, the affected erythrocytes contained normal amounts of haemoglobin.
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RIEDER, R., WOLF, D., CLEGG, J. et al. Rapid postsynthetic destruction of unstable haemoglobin Bushwick. Nature 254, 725–727 (1975). https://doi.org/10.1038/254725a0
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DOI: https://doi.org/10.1038/254725a0
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