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- W1618741211 abstract "Abstract The reaction of n-butyl isocyanide with deoxyhemoglobin A has been examined as a function of pH and ionic strength in the presence and absence of inositol hexaphosphate. In solutions of high pH (about 9) or of low ionic strength at pH 7 the rates of n-butyl isocyanide binding to the α and β chains within deoxyhemoglobin are almost equal. At pH 7, increase of ionic strength decreases the rate of binding to α chains. The addition of inositol hexaphosphate accentuates this effect, and in its presence the rates of binding and affinities of the α chains are substantially reduced in relation to the corresponding β chain values. Although it is known that organic phosphates bind between the β chains (Arnone, A. (1972) Nature 237, 146–149), the main effect of inositol hexaphosphate is a modification of the ligand-binding properties of the α chains. Similarly, the addition of protons to solutions of deoxyhemoglobin exerts a greater effect on the functional properties of the α chains than on the β chains, even though, at neutral pH 50% of the additional number of protons bound to deoxyhemoglobin are associated with the imidazole group of histidine 146 β (Kilmartin, J. V., and Wootton, J. F. (1970) Nature 228, 766–767). These results show that the functional properties of hemoglobin cannot be explained solely in terms of the perturbation of a single microscopic conformational equilibrium since the properties of the individual α and β chains within deoxyhemoglobin are unequally influenced by anions and protons while those of liganded hemoglobin are not." @default.
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- W1618741211 date "1973-03-01" @default.
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- W1618741211 title "The Effects of pH and Anions on the Properties of the α and β Chains within Human Deoxyhemoglobin" @default.
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- W1618741211 doi "https://doi.org/10.1016/s0021-9258(19)44235-x" @default.
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