The state of aggregation of human carbon monoxyhemoglobin in solution at neutral pH has been studied by light scattering at concentrations ranging from about 0.7 to 12 g/l. As in our earlier work, the scattering behavior at low ionic strength (0.1 M) indicates only intact tetrameric hemoglobin, and implies that the tetramer-dimer dissociation constant can be no more than about mol/l. In contrast, data I t appears well established that human adult hemoglobin (hemoglobin A) in the deoxy (Hb)' form does not dissociate appreciably into dimers, even in the presence of 2 M NaCl at neutral pH ; i.e., the tetramer-dimer dissociation constant is less than mol/l. (NorCn er ai., 1971; Kellett, 1971;Thomas and Edelstein, 1972). However, there remains disagreement on the dissociation of carbon monoxyhemoglobin,
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