Biomed Pap Med Fac Univ Palacky Olomouc Czech Repub. 2005, 149(2):261-264 | DOI: 10.5507/bp.2005.036

Isolation and purification of recombinant outer surface protein C (rOspC) of Borrelia burgdorferi Sensu Lato

Michal Křupkaa, Jana Bělákováa, Martina Šebestováa, Jana Tuháčkováb, Milan Raškaa, Vladimír Vrzalb, Evžen Weigla
a Department of Immunology, Faculty of Medicine, Palacký University, Olomouc
b Bioveta, a. s., Ivanovice na Hané

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.

Keywords: OspC, Borrelia burgdorferi, Recombinant protein, Immobilized metal ion affinity chromatography

Received: September 16, 2005; Accepted: November 11, 2005; Published: December 1, 2005  Show citation

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Křupka, M., Běláková, J., Šebestová, M., Tuháčková, J., Raška, M., Vrzal, V., & Weigl, E. (2005). Isolation and purification of recombinant outer surface protein C (rOspC) of Borrelia burgdorferi Sensu Lato. Biomedical papers, 149(2), 261-264. doi: 10.5507/bp.2005.036
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