The purification and characterisation of m-calpain from ostrich brain

Noxolo Mkwetshana, Ryno J. Naudé, Willem Oelofsen, Koji Muramoto, Takako Naganuma

    研究成果: Article査読

    3 被引用数 (Scopus)

    抄録

    Calpains are intracellular cysteine proteases activated in a Ca2+-dependent manner. The purpose of the present study was to investigate the physico-chemical and kinetic properties of ostrich brain m-calpain. m-Calpain was purified by successive chromatographic steps on Toyopearl-Super Q 650s and Pharmacia Mono Q HR 5/5 columns. A Ca2+ concentration of 5mM and a casein concentration of 5mg/ml were found to be necessary for optimum calpain activity. Ostrich m-calpain exhibited a Mr of 84K using SDS-PAGE and a Mmin of 79.3K from amino acid analysis. The pH and temperature optima were found to be 7.5 and 37°C, respectively. The amino acid composition of m-calpain revealed 700 residues. The N-terminal sequence of m-calpain showed sequence identity with chicken (27%), human (23%) and rabbit (18%) and Schistoma mansoni (9%).

    本文言語English
    ページ(範囲)337-347
    ページ数11
    ジャーナルInternational Journal of Biochemistry and Cell Biology
    34
    4
    DOI
    出版ステータスPublished - 2002

    ASJC Scopus subject areas

    • 生化学
    • 細胞生物学

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