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Oxygen Binding by Haemoglobin J-Cape Town (α2 92 Arg → Gln)

Nature volume 215, pages 297–298 (1967)Cite this article

Abstract

AN abnormal haemoglobin with the electrophoretic mobility of a haemoglobin J has been found in Cape Town, South Africa, and subsequently shown to be α2(92 Arg→Gln)β2 (ref. 1). The oxygen binding characteristics of this new haemoglobin are of particular interest because haemoglobin J-Chesapeake, which has the substitution Arg→Leu in the same position, has been shown to have an abnormally high affinity for oxygen2. Residue 92 of the α chain occupies the position 4 in the non-helical sequence between the helical segments which have been denoted by F and G (ref. 3), and it is in this area that the α and β chains are sliding past each other during oxygenation and deoxygenation of the haemoglobin molecule (personal communication from Perutz). A substitution of glutamine for arginine in this position can therefore be expected to influence the functional properties of the molecule and the haem–haem interaction.

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Authors and Affiliations

  1. John Bonnett Clinical Laboratories, Addenbrooke's Hospital, Cambridge

    J. G. LINES

  2. Medical Research Council, Abnormal Haemoglobin Research Unit, University Department of Biochemistry, Cambridge

    ROSALIND MCINTOSH

Authors
  1. J. G. LINES
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  2. ROSALIND MCINTOSH
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LINES, J., MCINTOSH, R. Oxygen Binding by Haemoglobin J-Cape Town (α2 92 Arg → Gln). Nature 215, 297–298 (1967). https://doi.org/10.1038/215297a0

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