Myofibril-Bound Serine Proteinase (MBP) and its Degradation of Myofibrillar Proteins

Authors

  • M.-J. Cao,

    Corresponding author
    1. Authors Cao, Hara, Osatomi, Izumi, and Ishihara are with the Dept. of Marine Biochemistry, Faculty of Fisheries, Nagasaki University, Bunkyo, Nagasaki 852-8521, Japan.
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  • K. Hara,

    1. Authors Cao, Hara, Osatomi, Izumi, and Ishihara are with the Dept. of Marine Biochemistry, Faculty of Fisheries, Nagasaki University, Bunkyo, Nagasaki 852-8521, Japan.
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  • K. Osatomi,

    1. Authors Cao, Hara, Osatomi, Izumi, and Ishihara are with the Dept. of Marine Biochemistry, Faculty of Fisheries, Nagasaki University, Bunkyo, Nagasaki 852-8521, Japan.
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  • K. Tachibana,

    1. Author Tachibana is with the Dept. of Fishery Nutritional Science, Faculty of Fisheries, Nagasaki Univ., Bunkyo, Nagasaki 852-8521, Japan.
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  • T. Izumi,

    1. Authors Cao, Hara, Osatomi, Izumi, and Ishihara are with the Dept. of Marine Biochemistry, Faculty of Fisheries, Nagasaki University, Bunkyo, Nagasaki 852-8521, Japan.
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  • T. Ishihara

    1. Authors Cao, Hara, Osatomi, Izumi, and Ishihara are with the Dept. of Marine Biochemistry, Faculty of Fisheries, Nagasaki University, Bunkyo, Nagasaki 852-8521, Japan.
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Address inquiries to Dr. M.-J. Cao.

ABSTRACT

Proteolysis of a myofibril-bound serine proteinase (MBP) from carp Cyprinus carpio on myofibrillar proteins and their gel formation ability were investigated. MBP readily decomposed myosin heavy chain as indicated by SDS-PAGE. In the preparation of kamaboko, the gel formation ability was diminished by addition of MBP. The optimum degradation temperatures of MBP to myosin heavy chain in myofibril and kamaboko gel were 55°C and 60°C, respectively. The degradation effects of MBP on actin, α-actinin and tropomyosin were studied by the immunoblotting method. Because of its myofibril-bound and myofibrillar protein degradation characteristics, MBP was regarded as the proteinase most probably involved in the modori effect.

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