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High Resolution Nuclear Magnetic Resonance Studies of Haemoglobin J Capetown

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Abstract

HAEMOGLOBIN J CAPETOWN1 is a Hb variant in which one amino-acid in the α-chain, arginine α92 (FG4), is replaced by glutamine. In Hb Chesapeake2 the same arginine is replaced by leucine, and the properties of the two variants are seen to be similar2,3. Compared with normal Hb A, both have increased oxygen affinities, smaller “haem-haem” interactions, and alkaline Bohr effects which are approximately normal. The X-ray crystallography of oxyhaemoglobin at 2.8 Å resolution, shows that the residue α92 (FG4) is at the α1βb2 interface4. Perutz and H. L.5 have pointed out that all known haemoglobin variants with alterations at the α1β2 interface have reduced “haem-haem” interaction.

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Authors and Affiliations

  1. Bell Telephone Laboratories, Inc., Murray Hill, New Jersey

    S. OGAWA & R. G. SHULMAN

  2. MRC Abnormal Haemoglobin Unit, University of Cambridge,

    P. A. M. KYNOCH & H. LEHMANN

Authors
  1. S. OGAWA
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  2. R. G. SHULMAN
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  3. P. A. M. KYNOCH
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  4. H. LEHMANN
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OGAWA, S., SHULMAN, R., KYNOCH, P. et al. High Resolution Nuclear Magnetic Resonance Studies of Haemoglobin J Capetown. Nature 225, 1042–1043 (1970). https://doi.org/10.1038/2251042a0

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  • DOI: https://doi.org/10.1038/2251042a0

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