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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References
German, B., and Wyman, J., J. Biol. Chem., 117, 533 (1937).
Kilmartin, J. V., and Rossi-Bernardi, L., Nature, 222, 1243 (1969).
Perutz, M. F., Muirhead, H., Mazzarella, L., Crowther, R. A., Greer, J., and Kilmartin, J. V., Nature, 222, 1240 (1969).
Benesch, R., and Benesch, R. E., J. Biol. Chem., 236, 405 (1961).
Geraci, G., Parkhurst, L. J., and Gibson, Q. H., J. Biol. Chem., 244, 4664 (1969).
Folk, J. E., Piez, K. A., Carroll, W. R., and Gladner, J. A., J. Biol. Chem., 235, 2272 (1960).
Antonini, E., Wyman, J., Zito, R., Rossi-Fanelli, A., and Caputo, A., J. Biol. Chem., 236, PC60 (1961).
Rossi-Bernardi, L., and Roughton, F. J. W., J. Biol. Chem., 242, 784 (1967).
Wyman, J., J. Biol. Chem., 127, 581 (1939).
Kilmartin, J. V., Wootton, J. F., and Hewitt, J. A. . (to be published).
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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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DOI: https://doi.org/10.1038/228766a0
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