Purification of the glycosylated beta subunit of (Na,K)-ATPase by lectin affinity chromatography
| Autor: | Earl T. Wallick, A. Ataei, Terence L. Kirley, M. J. Treuheit |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
Glycosylation
Chromatography biology Organic Chemistry Clinical Biochemistry Size-exclusion chromatography Lectin Biochemistry Wheat germ agglutinin Analytical Chemistry chemistry.chemical_compound chemistry Affinity chromatography Protein purification biology.protein Na+/K+-ATPase ATP synthase alpha/beta subunits |
| Zdroj: | Chromatographia. 33:521-524 |
| ISSN: | 1612-1112 0009-5893 |
| Popis: | Wheat germ agglutinin (WGA) affinity chromatography was examined as a method for the purification of the glycosylated beta subunit from SDS solubilized (Na,K)-ATPase. This lectin, WGA, bound quantitatively all of the beta subunit from SDS solubilized (Na,K)-ATPase whether or not the sample was reduced and/r alkylated. The combination of affinity and high performance size exclusion chromatography purified the beta subunit to a single band on SDS-PAGE electrophoresis. Compared to other methods of isolation this two step procedure utilizing wheat germ agglutinin was superior in terms of yield and purity for the beta subunit of (Na,K)-ATPase. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full text from SpringerLink