Affinity chromatography without immobilized ligands; A new method for studying macromolecular interactions using high-performance liquid chromatography
- 1 August 1982
- journal article
- research article
- Published by Elsevier in Analytical Biochemistry
- Vol. 124 (2) , 372-379
- https://doi.org/10.1016/0003-2697(82)90054-9
Abstract
No abstract availableFunding Information
- Ministry of Education, Culture, Sports, Science and Technology
This publication has 13 references indexed in Scilit:
- Theoretical aspects of DNA-protein interactions: Co-operative and non-co-operative binding of large ligands to a one-dimensional homogeneous latticePublished by Elsevier ,2004
- A new method for determining the dissociation constant between macromolecules by gel permeationAnalytical Biochemistry, 1981
- Multidimensional spectroscopic data correlation in the conformation transition of biological macromoleculesJournal of Biochemical and Biophysical Methods, 1980
- Separation range and separation efficiency in high-speed gel filtration on TSK-GEL SW columnsJournal of Chromatography A, 1980
- Isoelectric focusing of interacting systemsBiophysical Chemistry, 1979
- Quantitative uses of affinity chromatographyAnalytical Biochemistry, 1979
- A boundary sedimentation velocity method for determining nonspecific nucleic acid-protein interaction binding parametersAnalytical Biochemistry, 1977
- Cooperative elution of oligoadenylic acid in poly U immobilized chromatographyBiopolymers, 1975
- Theory of electrophoresis and sedimentation for some kinetically controlled interactionsBiochemistry, 1973
- A new form of chromatogram employing two liquid phasesBiochemical Journal, 1941