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Synthesis of haemoglobin Wayne in erythroid cells

Nature volume 269, pages 717–719 (1977)Cite this article

Abstract

HETEROZYGOTES for haemoglobin (Hb) Wayne possess two minor haemoglobin components that migrate more rapidly than HbA on electrophoresis at pH8.6. Each of the minor haemoglobin components contains an abnormal α chain in which the carboxyl-terminal tripeptide sequence, Lys-Tyr-Arg, has been replaced by an octapeptide1. The slower of the two components, henceforth designated Wayne-Asn, has the following octapeptide sequence: Asn-Thr-Val-Lys-Leu-Glu-Pro-Arg, whereas the faster one (Wayne-Asp) has exactly the same sequence except that asparagine at position 139 is replaced by aspartic acid. (These components, formerly designated1 Wayne-1 and Wayne-2, respectively, have been renamed for clarity.) This is the first variant described in which deamidation of the gene product is believed to occur. The purpose of this study was to demonstrate the proposed deamidation and to explain another interesting feature of the Hb Wayne phenotype in heterozygotes; namely, the presence of the variant haemoglobins in markedly reduced quantities relative to HbA (3% and 4%, respectively, for Hb Wayne-Asn and Hb Wayne-Asp).

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Authors and Affiliations

  1. Department of Human Genetics, University of Michigan Medical School, Ann Arbor, Michigan, 48109

    S. M. HANASH, W. P. WINTER & D. L. RUCKNAGEL

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  1. S. M. HANASH
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  2. W. P. WINTER
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  3. D. L. RUCKNAGEL
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HANASH, S., WINTER, W. & RUCKNAGEL, D. Synthesis of haemoglobin Wayne in erythroid cells. Nature 269, 717–719 (1977). https://doi.org/10.1038/269717a0

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