Results 171 to 180 of about 25,303 (208)
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Interactions between sickle hemoglobin fibers
Faraday Discussions, 2002We report on observations of "zippering" that occurs when two sickle hemoglobin fibers come together side by side. A transient Y-shaped object is formed which "zips " closed. We have been able to show how the strength of the interactions that drive this may be estimated by studying the frustrated structures sometimes formed between several fibers.
Christopher W, Jones +4 more
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Oxygen binding to sickle cell hemoglobin
Journal of Molecular Biology, 1979Abstract The extent of oxygen binding and light scattering of concentrated solutions of hemoglobin S have been determined as a function of oxygen partial pressure using a thin film optical cell. Nearly reversible oxygen binding is observed as witnessed by the small hysteresis found between slow deoxygenation and reoxygenation runs.
S J, Gill +4 more
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Interactions of Other Hemoglobin Variants with Sickle-Cell Hemoglobin
New England Journal of Medicine, 1970Deoxygenation-induced sickling of erythrocytes and gelling of hemolysates containing sickle-cell hemoglobin (Hb) are manifestations of the tendency of deoxyhemoglobin S in concentrated solutions to aggregate with the formation of gels or tactoids (liquid crystals).
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The Neurotoxic Effect of Sickle Cell Hemoglobin
Free Radical Research, 2004A growing body of experimental evidence suggests that the oxidative neurotoxicity of hemoglobin A may contribute to neuronal loss after CNS hemorrhage. Several hemoglobin variants, including hemoglobin S, are more potent oxidants in cell-free systems.
Garig M, Vanderveldt, Raymond F, Regan
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The oxygen equilibrium of sickle-cell hemoglobin
Biochimica et Biophysica Acta, 1961Abstract The equilibria between oxygen and normal and sickle-cell hemoglobins have been redetermined. Sickle-cell hemoglobin has a considerably lower affinity for oxygen than normal. At low concentrations the oxygen pressure at which sickle-cell hemoglobin is half oxygenated is 26–39% higher than in normal hemoglobin.
A, RIGGS, M, WELLS
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A New Hemoglobin Variant with Sickling Properties
New England Journal of Medicine, 1963THE red-cell sickling tendency of certain persons has long been a matter of great interest. Study of this problem by Pauling and his associates1 led to the suggestion of a genetic change in hemoglobin formation that resulted in synthesis of different globin fractions for normal and sickle-cell hemoglobin.
L E, PIERCE, C E, RATH, K, McCOY
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Ultrastructural Features of Erythrocyte and Hemoglobin Sickling
Archives of Internal Medicine, 1974Hemoglobin polymerization develops from a process of condensation, molecular interaction, aggregation, and assembly. Molecular organization of structures formed during polymerization depends on the type of hemoglobin, its specific defect, and its state of oxygenation. Sickling exemplifies hemoglobin polymerization.
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Stereospecific Inhibitors of the Gelation of Sickle Hemoglobin
Hemoglobin, 1980During the last decade there have been major advances in understanding the structure of the gel of deoxyhemoglobin S and the mechanism of its formation. These advances have allowed the development of a new strategy for the inhibition of gelation, i.e., stereospecific competitive inhibitors of the polymerization process.
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Screening for sickle hemoglobin??? a review
The American Journal of the Medical Sciences, 1973D W, Westring, S, Grand
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