Oxygen equilibria of hemoglobin A and hemoglobin S valency hybrids. |
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Authors: | J Murari |
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Institution: | 1. Chemistry Department, University of the West Indies, Kingston, Jamaica;2. Haematology Department, University College Hospital of the West Indies, Kingston, Jamaica |
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Abstract: | Oxygen equilibrium determinations with “unsymmetrical” MetHb/Hb hybrids derived from human hemoglobins A and S are reported. All four of the possible hybrids have higher oxygen affinity than the parent hemoglobins. The α2Metβ2S hybrid has a lower oxygen affinity than that of α2Metβ2S. However, both the βMet hybrids have similar oxygen affinity. The Bohr value of α2Metβ2S is more negative than that of α2Metβ2A while the βMet hybrids appear to have almost identical Bohr values. These findings favor the view that α and β chains in hemoglobin A have different conformations and indicate that hemoglobin S has a β-chain conformation different from that of β-chain of hemoglobin A. This difference is probably carried into the oxygenation properties of the α-chain in such a way as to be reflected only when the β chain is oxidized. |
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