Small angle neutron scattering studies of HbA in concentrated solutions.
Differential cross-sections for neutrons scattered by normal human hemoglobin have been determined over the range of concentrations from 2 to approximately 35 weight percent. Data are compared with structure factors calculated from models of monodisperse hard spheres interacting through a screened Coulomb potential. Good agreement is noted when the volume fraction eta is adjusted during multivariate fitting of data, but the fitted value of eta is always lower than expected from the known Hb concentration of the samples. Calculations of cross-sections for polydisperse scatterers suggest that the samples may contain oligomers of the fundamental tetrameric Hb molecule.
University of Maryland, College Park 20742.
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Krueger
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Chen
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Hofrichter
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Nossal
D002263:Carboxyhemoglobin / Q000737:chemistry*; D006441:Hemoglobin A / Q000737:chemistry*; D006801:Humans; D009502:Neutrons; D011487:Protein Conformation; D012542:Scattering, Radiation
D006441:Hemoglobin A; D002263:Carboxyhemoglobin