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• W2014046119 abstract "We have determined the low temperature EPR spectra and room temperature ligand dissociation rate constants of human NO-hemoglobins F and A as a function of pH and inositol hexaphosphate levels in order to assess the contribution of a quaternary structural equilibrium in the two proteins to their spectral and functional properties. Our results are consistent with an increased stability of a ligated low affinity structure in the fetal protein; the functional properties of this structure appear to be essentially the same in the two hemoglobins, even though its stability relative to a high affinity conformation is different. The pH dependence of the NO dissociation constant in both adult and fetal hemoglobin can be assigned primarily to the pH-dependent equilibria of high and low affinity forms as monitored by EPR." @default.
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• W2014046119 date "1978-05-02" @default.
• W2014046119 modified "2023-09-26" @default.
• W2014046119 title "Analogous effect of protons and inositol hexaphosphate on the alteration of structure of nitrosyl fetal human hemoglobin" @default.
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• W2014046119 doi "https://doi.org/10.1021/bi00602a025" @default.
• W2014046119 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26386" @default.
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