Journal article
Oxygen binding by sickle cell hemoglobin polymers
Journal of molecular biology, v 158(2), pp 251-273
1982
PMID: 7120411
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
The thermodynamics of sickle cell hemoglobin gelation in the presence of oxygen has been investigated by measuring the fractional saturation of the solution and polymer phases, and the solubility. The fractional saturation of the solution phase with oxygen and the solubility were measured by near infrared spectrophotometry after sedimentation of the polymers, while the fractional saturation of the polymer phase was determined from linear dichroism measurements on gels formed by nucleation with an argon ion laser. Using the solution binding data of Gill
et al. (1979) to calculate the oxygen pressure corresponding to the solution phase saturation, the initial portion of the polymer binding curve was determined. The self-consistency of the data analysis in terms of the two-phase model for the gel was tested by comparing measured and calculated gel (i.e. solution plus polymer) binding curves, and by comparing the observed solubilities with those calculated from the solution and polymer binding curves using Gibbs-Duhem relations.
Oxygen binding to the polymer was found to be non-co-operative up to the maximum measured fractional saturation of 0.14. The binding constant was 0.0059 ± 0.0015 torr
−1 (
p
50 = 170 ± 40 torr), which is about three times smaller than that of hemoglobin in the low-affinity T quaternary structure. Both the non-co-operative binding and the low affinity could be qualitatively explained in terms of an allosteric model and the current information on the polymer structure.
Metrics
Details
- Title
- Oxygen binding by sickle cell hemoglobin polymers
- Creators
- Helen R. Sunshine - National Institute of Diabetes and Digestive and Kidney DiseasesJames Hofrichter - National Institute of Diabetes and Digestive and Kidney DiseasesFrank A. Ferrone - National Institute of Diabetes and Digestive and Kidney DiseasesWilliam A. Eaton - National Institute of Diabetes and Digestive and Kidney Diseases
- Publication Details
- Journal of molecular biology, v 158(2), pp 251-273
- Publisher
- Elsevier
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Physics
- Web of Science ID
- WOS:A1982NU89500006
- Scopus ID
- 2-s2.0-0020318201
- Other Identifier
- 991019238730804721
UN Sustainable Development Goals (SDGs)
This publication has contributed to the advancement of the following goals:
InCites Highlights
Data related to this publication, from InCites Benchmarking & Analytics tool:
- Web of Science research areas
- Biochemistry & Molecular Biology