Use of high-performance size-exclusion, ion-exchange, and hydrophobic interaction chromatography for the measurement of protein conformational change and stability
- 1 January 1987
- journal article
- research article
- Published by Elsevier in Journal of Chromatography A
- Vol. 398, 175-202
- https://doi.org/10.1016/s0021-9673(01)96504-5
Abstract
No abstract availableThis publication has 78 references indexed in Scilit:
- Quantitative Determination of the α-Amylase Inhibitor fromPhaseolus Vulgarisusing size Exclusion High-Performance Liquid ChromatographyJournal of Liquid Chromatography, 1984
- Comparison of the rates of inactivation and conformational changes of creatine kinase during urea denaturationBiochemistry, 1984
- Analysis and Control of Protein and Polypeptide DrugsDrug Development and Industrial Pharmacy, 1984
- Monitoring of the elution from a high-performance gel chromatography column by a spectrophotometer, a low-angle laser light scattering photometer and a precision differential refractometer as a versatile way to determine protein molecular weightJournal of Chromatography A, 1983
- Characterization of Protein-Protein and Protein-Ligand Interactions by High Performance Size Exclusion ChromatographyJournal of Liquid Chromatography, 1982
- Biological activity and conformational stability of the domains of plasma fibronectinArchives of Biochemistry and Biophysics, 1981
- Circular dichroism and the conformational properties of soybean β-amylaseArchives of Biochemistry and Biophysics, 1981
- Reverse-phase high-performance liquid chromatography of proteins: The separation of hemoglobin chain variantsAnalytical Biochemistry, 1980
- High-performance liquid chromatography of proteinsAnalytical Biochemistry, 1980
- Bovine serum albumin as a catalyst. III. Conformational studiesJournal of the American Chemical Society, 1975