Electrophoretic mobilities of the complexes between sodium dodecyl sulfate and various peptides or proteins determined by free solution electrophoresis using coated capillaries
- 1 January 1994
- journal article
- research article
- Published by Wiley in Electrophoresis
- Vol. 15 (1) , 1141-1146
- https://doi.org/10.1002/elps.11501501172
Abstract
Electrophoretic mobilities of various proteins or peptides complexed with sodium dodecyl sulfate (SDS) were determined by free solution capillary electrophoresis. The complexes formed between SDS and protein polypeptide showed electrophoretic mobilities virtually insensitive to the protein molecular weight. On the other hand, scattered and larger negative electrophoretic mobilities were observed for peptides of molecular weights less than 10000. Mobility differences as small as 0.3–3% among the three differently modified derivatives of bovine serum albumin could also be successfully determined due to the high resolving power of capillary electrophoresis.Keywords
This publication has 7 references indexed in Scilit:
- High-performance capillary electrophoresis of SDS-protein complexes using UV-transparent polymer networksAnalytical Chemistry, 1992
- Calculation of the isoelectric points of polypeptides from the amino acid compositionTrAC Trends in Analytical Chemistry, 1986
- High-performance electrophoresisJournal of Chromatography A, 1985
- A simple method for displaying the hydropathic character of a proteinJournal of Molecular Biology, 1982
- Binding Isotherms of Sodium Dodecyl Sulfate to Protein Polypeptides with Special Reference to SDS-polyacylamide Gel ElectrophoresisThe Journal of Biochemistry, 1975
- Measurement of Free Electrophoretic Mobility and Retardation Coefficient of Protein-Sodium Dodecyl Sulfate Complexes by Gel ElectrophoresisPublished by Elsevier ,1972
- The Preparation and Enzymatic Hydrolysis of Reduced and S-Carboxymethylated ProteinsJournal of Biological Chemistry, 1963