Abstract
STUDIES of abnormal human haemoglobins (Hbs) with increased O2 affinity have been particularly useful in developing detailed molecular interpretations of normal Hb function. A number of functionally interesting mutants are altered in the βHC region but only one variant, Hb Hiroshima (β146 His→Asp)1,2, has been reported as having a substitution at the C terminus itself. We report here the structure and O2 equilibria of Hb York, a new mutation at the β146 position, His→Pro, associated with increased O2 affinity, decreased cooperativity and diminished Bohr effect.
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BARE, G., BROMBERG, P., ALBEN, J. et al. Altered C-terminal salt bridges in haemoglobin York cause high oxygen affinity. Nature 259, 155–156 (1976). https://doi.org/10.1038/259155a0
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DOI: https://doi.org/10.1038/259155a0
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