Počet záznamů: 1  

Purification and crystallization of human Cu/Zn superoxide dismutase recombinantly produced in the protozoan Leishmania tarentolae

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    SYSNO ASEP0347295
    Druh ASEPJ - Článek v odborném periodiku
    Zařazení RIVJ - Článek v odborném periodiku
    NázevPurification and crystallization of human Cu/Zn superoxide dismutase recombinantly produced in the protozoan Leishmania tarentolae
    Tvůrce(i)Gazdag, E. M. (DE) - Cirstea, I. (DE) - Breitling, R. (DE) - Lukeš, Julius (BC-A) - Blankenfeldt, W. (DE) - Alexandrov, K. (AU)
    Rozsah stran871 - 877
    Zdroj.dok.Acta Crystallographica Section F - ISSN 1744-3091
    Poč.str.7 s.
    Jazyk dok.eng - angličtina
    Země vyd.GB - Velká Británie
    Klíč. slovarecombinant proteins ; eukaryotic expression systems ; Leishmania
    Vědní obor RIVEB - Genetika a molekulární biologie
    CEZAV0Z60220518 - PAU-O, BC-A (2005-2011)
    UTISI000280708200002
    DOI10.1107/S1744309110019330
    AnotaceThe rapid and inexpensive production of high-quality eukaryotic proteins in recombinant form still remains a challenge in structural biology. Here, a protein-expression system based on the protozoan Leishmania tarentolae was used to produce human Cu/Zn superoxide dismutase (SOD1) in recombinant form. Sequential integration of the SOD1 expression cassettes was demonstrated to lead to a linear increase in expression levels to up to 30 mg per litre. Chromatographic purification resulted in 90% pure recombinant protein, with a final yield of 6.5 mg per litre of culture. The protein was crystallized and the structures of two new crystal forms were determined. These results demonstrate the suitability of the L. tarentolae expression system for structural research.
    PracovištěBiologické centrum (od r. 2006)
    KontaktVáclava Lavičková, lavickova@hbu.cas.cz, Tel.: 387 775 889
    Rok sběru2011