Optical rotatory dispersion and sedimentation in the study of association-dissociation: Bovine β-lactoglobulins near pH5
- 1 September 1967
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure
- Vol. 147 (1) , 73-92
- https://doi.org/10.1016/0005-2795(67)90091-8
Abstract
No abstract availableThis publication has 39 references indexed in Scilit:
- Milk ProteinsPublished by Elsevier ,1967
- Liver Enzymes in Biliary RetentionNature, 1962
- Molecular Interactions in β-Lactoglobulin. III. Light Scattering Investigation of the Stoichiometry of the Association between pH 3.7 and 5.22Journal of the American Chemical Society, 1960
- Molecular Interactions in β-Lactoglobulin. II. Ultracentrifugal and Electrophoretic Studies of the Association of β-Lactoglobulin below its Isoelectric Point2Journal of the American Chemical Society, 1960
- The solubility and fractionation of β1-lactoglobulinBiochemical Journal, 1957
- Genetics of the β-Lactoglobulins of Cow's MilkNature, 1957
- The heterogeneity of bovine β-lactoglobulinBiochemical Journal, 1957
- The pH dependence of the association of β-lactoglobulinArchives of Biochemistry and Biophysics, 1956
- Occurrence of Different Beta-Lactoglobulins in Cow's MilkNature, 1955
- Studies on the heterogeneity of crystallized β-lactoglobulinBiochemical Journal, 1955