Purification and partial characterization of a myofibril-bound serine protease from ostrich skeletal muscle

Shonisani C. Tshidino, Jason Krause, Abayomi P. Adebiyi, Koji Muramoto, Ryno J. Naudé

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    3 Citations (Scopus)


    A myofibril-bound serine protease (MBSP) was partially purified from ostrich (Struthio camelus) skeletal muscle. MBSP was dissociated from the myofibrillar fraction by ethylene glycol treatment at pH 8.5, followed by partial purification via Toyopearl Super Q 650 S and p-aminobenzamidine column chromatographies. Ostrich MBSP revealed a major protein band of approximately 21 kDa on SDS-PAGE, showing proteolytic activity after casein zymography. Optima pH and temperature of ostrich MBSP were 8 and 40 °C, respectively. Substrate specificity analysis revealed that the enzyme cleaved synthetic fluorogenic substrates at the carboxyl side of arginine residues. Kinetic parameters (Km and Vmax values) were calculated from Lineweaver-Burk plots. The kinetic characteristics of ostrich MBSP were compared to values obtained for commercial bovine trypsin in this study, as well as those obtained for MBSP from mouse and various fish species. The results suggest that ostrich MBSP is a tryptic-like serine protease. Ostrich MBSP exhibited low sequence identity to commercial bovine trypsin (44%), MBSP from lizard fish skeletal muscle (33%) and trypsinogen from ostrich pancreas (22%).

    Original languageEnglish
    Pages (from-to)229-234
    Number of pages6
    JournalComparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
    Issue number2
    Publication statusPublished - 2009 Oct


    • Bovine trypsin
    • Myofibril-bound serine protease
    • Myofibrils
    • Ostrich

    ASJC Scopus subject areas

    • Biochemistry
    • Physiology
    • Molecular Biology


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