Book chapter
Oxygen Binding and the Gelation of Sickle Cell Hemoglobin
The Molecular Basis of Mutant Hemoglobin Dysfunction, pp 225-236
1981
Abstract
The thermodynamics of gelation of hemoglobin S partially saturated with oxygen have been investigated. The total concentration (solubility) and fractional saturation of the solution phase in equilibrium with polymerized hemoglobin was determined by near-infrared spectrophotometry after sedimentation of the polymers. The fractional saturation of the aligned polymer phase was determined from linear dichroism measurements. Using this data and the two-phase model for the gel, we calculate gel binding curves which agree well with those recently reported by Gill et al. (J. Mol. Biol. 130:175, 1979) confirming the validity of the two-phase model. The polymer binding curve is noncooperative and can be explained by an allosteric model in which no R-state molecules polymerize, and T-state molecules are excluded from the polymer by about 600 calories/mole for each molecule of oxygen bound.
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Details
- Title
- Oxygen Binding and the Gelation of Sickle Cell Hemoglobin
- Creators
- J. Hofrichter - National Institute of Arthritis and Musculoskeletal and Skin DiseasesH.R. Sunshine - National Institute of Arthritis and Musculoskeletal and Skin DiseasesF.A. Ferrone - Drexel UniversityW.A. Eaton - National Institute of Arthritis and Musculoskeletal and Skin Diseases
- Publication Details
- The Molecular Basis of Mutant Hemoglobin Dysfunction, pp 225-236
- Publisher
- Elsevier
- Resource Type
- Book chapter
- Language
- English
- Academic Unit
- Physics
- Other Identifier
- 991019238552504721