The purification and characterisation of m-calpain from ostrich brain

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

    Research output: Contribution to journalArticlepeer-review

    3 Citations (Scopus)


    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%).

    Original languageEnglish
    Pages (from-to)337-347
    Number of pages11
    JournalInternational Journal of Biochemistry and Cell Biology
    Issue number4
    Publication statusPublished - 2002


    • Brain
    • Calcium
    • Ostrich
    • m-Calpain

    ASJC Scopus subject areas

    • Biochemistry
    • Cell Biology


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