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Inhibition of Bohr Effect after Removal of C-Terminal Histidines from Haemoglobin β-Chains

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Abstract

THE alkaline Bohr effect is the uptake of protons at a pH greater than 6 when oxygen is removed from haemoglobin1. In horse haemoglobin the α-amino groups of the α-chain contribute about one-quarter of the alkaline Bohr effect2. Recently Perutz et al.3 proposed that histidine 146β contributes about half the alkaline Bohr effect. Their evidence was based on the interpretation of a difference Fourier map of deoxyhaemoglobin after reaction with N-ethylmaleimide4. This haemoglobin has lost half its alkaline Bohr effect. We have prepared des-(His 146β) human haemoglobin: it exhibits haem-haem interaction and lacks half the alkaline Bohr effect, and thus fully confirms the ideas of Perutz et al.3.

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Author notes

  1. J. F. WOOTTON

    Present address: Department of Physiology, Biochemistry and Pharmacology, Veterinary College, Cornell University, Ithaca, New York, 14850

Authors and Affiliations

  1. MRC Laboratory of Molecular Biology, Hills Road, Cambridge

    J. V. KILMARTIN & J. F. WOOTTON

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  1. J. V. KILMARTIN
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  2. J. F. WOOTTON
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KILMARTIN, J., WOOTTON, J. Inhibition of Bohr Effect after Removal of C-Terminal Histidines from Haemoglobin β-Chains. Nature 228, 766–767 (1970). https://doi.org/10.1038/228766a0

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