Self-association in highly concentrated solutions of myoglobin: a novel analysis of sedimentation equilibrium of highly nonideal solutions
- 1 December 1981
- journal article
- research article
- Published by Elsevier in Biophysical Chemistry
- Vol. 14 (4), 317-324
- https://doi.org/10.1016/0301-4622(81)85033-8
Abstract
No abstract availableThis publication has 10 references indexed in Scilit:
- Evidence for protein self-association induced by excluded volume Myoglobin in the presence of globular proteinsBiochimica et Biophysica Acta (BBA) - Protein Structure, 1981
- Thermodynamic nonideality and the dependence of partition coefficient upon solute concentration in exclusion chromatographyBiophysical Chemistry, 1980
- The effect of non-aggregating proteins upon the gelation of sickle cell hemoglobin: Model calculations and data analysisBiochemical and Biophysical Research Communications, 1979
- Temperature dependence of nonideality in concentrated solutions of hemoglobinBiopolymers, 1978
- Intermolecular effects in the polymerization of hemoglobin SBiochemical and Biophysical Research Communications, 1978
- Analysis of non-ideal behavior in concentrated hemoglobin solutionsJournal of Molecular Biology, 1977
- Effects of pH, 2,3-diphosphoglycerate and salts on gelation of sickle cell deoxyhemoglobinJournal of Molecular Biology, 1973
- Concerted Formation of the Gel of Hemoglobin SProceedings of the National Academy of Sciences, 1973
- Equilibrium sedimentation studies of the aggregation of methylene blueThe Journal of Physical Chemistry, 1972
- The properties and interactions of the isolated α and β chains of human haemoglobinJournal of Molecular Biology, 1965