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- W2023846617 abstract "Protease activity of rat gastrocnemius myofibrillar fraction, optimally active at the alkaline pH range, was investigated. The activity was inhibited by soybean trypsin inhibitor, tranexamic acid and other inhibitors of proteases, as well as by 2- to 10-mm solutions of FeCl2, FeCl3, and ZnCl2. CaCl2, MgCl2, and MnCl2 at the same concentration range did not affect the activity of the enzyme. Treating the myofibrillar fraction with 1 m KCNS or KCl solubilized the enzyme. The protease activity was increased after 4 days of fasting, and on Day 6 was five times higher than in nonfasted rats. This increase in specific activity was significant when expressed in terms of total protein, noncollagen protein, or muscle DNA content. Protease activity also increased in rats after glucocorticoid administration, in rats with alloxan diabetes, in aminonucleoside-nephrotic rats, and in rats with hypoproteinemia induced by plasmapheresis. These findings suggest that the activity of the myofibrillar protease is adaptive, and increases whenever catabolism of muscle proteins and mobilization of amino acids to the liver is required." @default.
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- W2023846617 date "1974-03-01" @default.
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- W2023846617 title "Rat myofibrillar protease: Enzyme properties and adaptive changes in conditions of muscle protein degradation" @default.
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- W2023846617 doi "https://doi.org/10.1016/0003-9861(74)90230-6" @default.
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