Isolation and purification of recombinant outer surface protein C (rOspC) of Borrelia burgdorferi sensu lato
Language English Country Czech Republic Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
16601766
DOI
10.5507/bp.2005.036
Knihovny.cz E-resources
- MeSH
- Antigens, Bacterial biosynthesis isolation & purification MeSH
- Vaccines, DNA biosynthesis isolation & purification MeSH
- Escherichia coli MeSH
- Genetic Vectors MeSH
- Bacterial Outer Membrane Proteins biosynthesis isolation & purification MeSH
- Lyme Disease Vaccines biosynthesis isolation & purification MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Antigens, Bacterial MeSH
- Vaccines, DNA MeSH
- OspC protein MeSH Browser
- Bacterial Outer Membrane Proteins MeSH
- Lyme Disease Vaccines MeSH
The aim of this work was isolation and purification of the major immunodominant protein, Outer surface protein C (OspC) of three members of the species group Borrelia burgdorferi, the causative agent of Lyme disease. Our aim was to obtain this protein in a quantity and purity sufficient for immunization of experimental animals. For optimalization of protein purification's yield we used immobilized metal ion affinity chromatography (IMAC) under different conditions. The greatest efficiency was achieved by using of HiTrap Chelating Column under native conditions.
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