Durchschlag, H. and Jaenicke, Rainer (1997) SDS-electrophoresis of glycoproteins. CHIMICA OGGI-CHEMISTRY TODAY, 15 (9-10). pp. 15-24. ISSN 0392-839X, 1973-8250
Full text not available from this repository.Abstract
The most popular method for estimating the molecular weight of a polypeptide chain is the measurement of its mobility by polyacrylamide gel electrophoresis in the presence of the anionic detergent sodium dodecyl sulfate. The application of the method to glycoproteins of other conjugated proteins, however; poses several problems, primarily due to the occurrence of an abnormal migration behavior. In the case of glycoproteins, the aberrant electrophoretic migration is due to the special molecular features of the glycan chains which may cause complex interactions with the gel matrix. In order to unveil possible reasons for these electrophoretic peculiarities, a series of glycoproteins of varying carbohydrate content and molar mass were studied, together with non-conjugated proteins as references. Both electrophoresis conditions and evaluation methods were varied systematically. The application of different values for the electrophoretic parameters T and C (reflecting gel concentration and crosslinking) allowed a detailed physico-chemical analysis, e.g. in terms of Ferguson and Segrest plots. The results show how interpretative difficulties encountered with glycoproteins or other compounds with aberrant migration behavior can be avoided by simple precautions. These may also be used for non-conjugated proteins when striving for more accurate results of electrophoretic analyses.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | SODIUM-DODECYL-SULFATE; MOLECULAR-WEIGHT ESTIMATION; POLYACRYLAMIDE-GEL ELECTROPHORESIS; PORE GRADIENT ELECTROPHORESIS; PROTEINS; SEPARATION; COMPLEXES |
| Subjects: | 500 Science > 540 Chemistry & allied sciences 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 30 Mar 2023 05:20 |
| Last Modified: | 30 Mar 2023 05:20 |
| URI: | https://pred.uni-regensburg.de/id/eprint/50589 |
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