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Connectin content and its post-mortem changes in fish muscle.

N Seki, T Watanabe

    Journal of Biochemistry
    |April 1, 1984
    PubMed
    Summary
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    Connectin, a protein in fish and rabbit muscle, changes during aging. Carp muscle shows faster changes in connectin composition compared to rabbit muscle.

    Area of Science:

    • Muscle protein research
    • Comparative biochemistry

    Background:

    • Connectin is a high molecular weight protein found in myofibrils.
    • Its role and changes during post-mortem aging are not fully understood across species.

    Purpose of the Study:

    • To compare the content and characteristics of connectin in fish and rabbit skeletal muscles.
    • To investigate the effects of post-mortem aging on connectin submolecular composition in different species.

    Main Methods:

    • Isolation of connectin from fish and rabbit myofibrils using SDS-gel filtration.
    • Analysis of connectin composition via SDS-polyacrylamide gel electrophoresis.
    • Monitoring changes in connectin bands during post-mortem muscle aging.

    Main Results:

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    • Connectin constitutes about 13% of fish myofibrillar proteins and 16% in rabbits, with no significant species variation in fish.
    • High molecular weight connectins from carp and rabbit exhibit a doublet band (bands 1 and 2), with rabbit band 1 migrating slower than carp band 1.
    • Post-mortem aging caused band 1 to decrease and band 2 to increase, with further transformation into faster bands, indicating similar aging effects on carp and rabbit connectin.

    Conclusions:

    • Connectin content is similar across fish species and comparable to rabbits.
    • Post-mortem aging affects connectin structure similarly in fish and mammals.
    • Carp muscle exhibits a faster rate of connectin band 1 degradation during aging compared to rabbit muscle.