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• W2076131092 abstract "A small-angle neutron scattering study of Lumbricus terrestris hemoglobin in solution at neutral pH was carried out. The results were interpreted in terms of several models for the subunit structure. The best fit is consistent with a hexagonal bilayer model made up of 12 spherical subunits, approx. 48 Å in radius, each represented by an aggregate of 19 small spheres of approx. 16.7 Å. in radius. The scattering of hemoglobin, briefly subjected to alkaline pH or to heating, was also measured in order to determine whether any alterations in dimensions accompanied a decrease in the cooperativity of oxygen binding. It was found that an exposure of 20 min to 0.1 M sodium borate buffer (pH 9) resulted in no change in the elution volume in Sepharose CL-6B gel filtration, and only minor changes in the observed neutron scattering at high angles; however, the exposure led to an irreversible decrease in the Hill constant from about 3.5 to 2.2. Heating produced irreversible and marked alteration both in the scattering from the hemoglobin and in its oxygen binding, accompanied by partial aggregation and denaturation." @default.
• W2076131092 created "2016-06-24" @default.
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• W2076131092 date "1982-12-01" @default.
• W2076131092 modified "2023-09-26" @default.
• W2076131092 title "Small-angle neutron scattering study of the molecular subunit structure of earthworm hemoglobin Effects of alkaline pH and thermal denaturation" @default.
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• W2076131092 doi "https://doi.org/10.1016/0167-4838(82)90430-7" @default.
• W2076131092 hasPublicationYear "1982" @default.
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