Comparison of different transition metal ions for immobilized metal affinity chromatography of selenoprotein P from human plasma
| Autor: | O. Farver, Ole Jøns, Ulrik Sidenius, Bente Gammelgaard |
|---|---|
| Rok vydání: | 2000 |
| Předmět: |
inorganic chemicals
Affinity label Ion chromatography Chromatography Affinity Affinity chromatography Nickel Selenoprotein P Humans Amino Acid Sequence Selenoproteins Inductively coupled plasma mass spectrometry chemistry.chemical_classification Chromatography biology Chemistry Sepharose Proteins Fast protein liquid chromatography Affinity Labels General Chemistry Cobalt Displacement chromatography Molecular Weight Zinc Metals biology.protein Electrophoresis Polyacrylamide Gel Selenoprotein Copper Cadmium |
| Zdroj: | University of Copenhagen |
| ISSN: | 1387-2273 |
| Popis: | Cu2+, Ni2+, Zn2+, Co2+ and Cd2+ were evaluated in metal ion affinity chromatography for enrichment of selenoprotein P, and immobilized Co2+ affinity chromatography was found to be the most selective chromatographic method. The chromatography was performed by fast protein liquid chromatography and the fractionation was followed by analysis of the collected fractions for selenium by inductively coupled plasma mass spectrometry. By the combination of immobilized Co2+ affinity chromatography and heparin affinity chromatography a simple method was developed yielding a 14,800-fold enrichment of selenoprotein P. The purity of the protein was determined by SDS-PAGE and by sequencing from polyvinylidene difluoride blots of SDS-PAGE gels. |
| Databáze: | OpenAIRE |
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