Interchain disulfide bonds in immunoglobulins: Analysis by two-dimensional polyacrylamide-gel electrophoresis
| Autor: | Frank F. Richards, B.N. Manjula |
|---|---|
| Rok vydání: | 1975 |
| Předmět: |
Macromolecular Substances
Protein Conformation Biophysics Immunoglobulin light chain Biochemistry Cell Line Mice chemistry.chemical_compound Methods Animals Disulfides Molecular Biology Polyacrylamide gel electrophoresis Gel electrophoresis Mice Inbred BALB C Binding Sites Chromatography biology Disulfide bond Sodium Dodecyl Sulfate Cell Biology Immunoglobulin A Molecular Weight Electrophoresis Crystallography Myeloma Proteins chemistry Acrylamide biology.protein Electrophoresis Polyacrylamide Gel Rabbits gamma-Globulins Antibody Protein Binding |
| Zdroj: | Analytical Biochemistry. 66:412-422 |
| ISSN: | 0003-2697 |
| DOI: | 10.1016/0003-2697(75)90609-0 |
| Popis: | The arrangement of interchain disulfide bonds in immunoglobulins may be determined in a single experiment by two-dimensional SDS-polyacrylamide-gel electrophoresis. The noncovalently associated subunits are first separated on a cylindrical acrylamide-gel by electrophoresis under dissociating conditions. The subunits are then subjected to reduction in situ followed by electrophoresis on a slab gel of acrylamide in a direction perpendicular to the first to separate the constituent polypeptide chains (heavy and/or light chains) of the individual subunits. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|