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  • Efficient removal of cathepsin L from active cathepsin X using immunoprecipitation technique
    Pečar Fonović, Urša ; Kos, Janko, 1959-
    Cathepsin X is a cysteine protease which is involved in various important physiological and pathological processes. For the purpose of biochemical and structural studies, pure and active cathepsin X ... is required without contamination with other related proteases. Recombinant cathepsin X was obtained by expression in methylotropic yeast Pichia pastoris. During purification, cathepsin X has to be activated with cysteine protease cathepsinL, however, separation methods, used so far, can not completely remove cathepsin L from the activated cathepsin X. Here we describe a new purification procedure which provides active recombinant cathepsin X without the presence of residual cathepsin L.
    Vir: Acta chimica slovenica. - ISSN 1318-0207 (Vol. 56, no. 4, 2009, str. 985-988)
    Vrsta gradiva - članek, sestavni del
    Leto - 2009
    Jezik - angleški
    COBISS.SI-ID - 2730353

    Povezava(-e):

    Digitalna knjižnica Slovenije - dLib.si

vir: Acta chimica slovenica. - ISSN 1318-0207 (Vol. 56, no. 4, 2009, str. 985-988)

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