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- W2045084934 abstract "To investigate the effects of lysosomal proteases on myofibril fragmentation, tilapia (Tilapia nilotica X T. aurea) muscle myofibrils were incubated with isolated lysosomal fraction containing 12 units of cathepsin D/mL (G-II) and pure cathepsin D (12 units/mL G-III) at pH 5.5, 6.0, and 6.5 for 3 days at 4°C. Among samples incubated at pH 5.5, the degree of myofibril fragmentation (DMF) of G-III was highest, while, at pH 6.0 and 6.5, that of G-II was highest. At pH 6.5, the higher DMF of G-III than that of G-I suggested that cathepsin D still had proteolytic activity on myofibrils. Difference in the decrease of protein content between G-III and G-I, and between G-II and G-I indicated that proteolysis caused by cathepsin D was highest at pH 5.5, while that caused by lysosomal enzymes was highest at pH 6.5. This suggested the participation of lysosomal enzymes in the fragmentation of myofibrils." @default.
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- W2045084934 date "1992-03-01" @default.
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- W2045084934 title "Lysosomal Enzyme Effects on the Postmortem Changes in Tilapia (Tilapia nilotica X T. aurea) Muscle Myofibrils" @default.
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- W2045084934 doi "https://doi.org/10.1111/j.1365-2621.1992.tb05475.x" @default.
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