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- W1636679432 abstract "The values of pKa for β-146 and β-2 histidines in human hemoglobin were determined by the mass spectrometric method using the hydrogen-deuterium exchange reaction. The effects of ligand binding and allosteric interaction on these pKa values were investigated. The pKa values of β-146 histidine in the oxy- and deoxy-forms of the stripped hemoglobin were little affected by addition of inositol hexaphosphate (7.0 in the oxy- and 8.2 in the deoxy form). Blocking of the reactive thiol group at β-93 cysteine decreased the pKa values of the amino acid remarkably in both the oxy- and deoxy-forms, whereas the difference in pKa between the oxy- and deoxy-forms (ΔpKa remained unchanged. Values of the pKa in the tetramer of the β-chain were found to be 7.4 in both the oxy- and deoxy-forms. The pKa value in methemoglobin was found to be 7.0. Values of pKa of β-2 histidine on human hemoglobin were measured mass-spectrometrically after isolation of histidine as the methyl thiohydantoin derivative from deuterated hemoglobin by stepwise Edman degradation. From these measurements a pKa value of 6.9 for this histidine in both oxy- and deoxy-hemoglobin was found in the absence of inositol hexaphosphate. The pKa. value of the histidine in oxyhemoglobin was little affected by inositol hexaphosphate, while the value in deoxyhemoglobin was shifted to a higher value of 7.7 by inositol hexaphosphate." @default.
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- W1636679432 date "1977-09-01" @default.
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- W1636679432 title "Studies on the Heterotropic Interaction of Hemoglobin1" @default.
- W1636679432 doi "https://doi.org/10.1093/oxfordjournals.jbchem.a131759" @default.
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