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- W2000792248 abstract "1. The specific activity of soluble (lipid-free) succinic dehydrogenase isolated from the epaxial muscle of goldfish acclimated to both 5 and 25°C was increased by incubation with soluble lipid preparations 2. A total mitochondrial lipid extract from 5°C-acclimated goldfish was a more effective reactivator of the enzyme (from either 5− or 25°C-acclimated goldfish) than a comparable extract from 25°C-acclimated goldfish (reactivation of 142±3·3 vs. 128±2·3 per cent; this difference was referable to the greater degree of unsaturation of the 5°C-lipid extract. 3. Studies with highly purified phopholipids indicated that the affinity of the enzyme for lipid was largely dependent upon the phosphatide species, whereas the magnitude of the reactivation was dependent primarily upon the degree of unsaturation of the fatty acid residues. 4. Reactivation of the soluble dehydrogenase was accompanied by an increase in both the Krmm for succinate and Vmax and a restoration of the Km∼-temperature characteristics of the native (particulate) enzyme; changes in Km upon reactivation were not lipid specific. 5. These results were interpreted as indicating that the increased specific activity of succinic dehydrogenase following a period of cold acclimation may be partly or in large part explained by underlying changes in membrane composition which regulate the activity rather than the quantity of this enzyme." @default.
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- W2000792248 date "1972-12-01" @default.
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- W2000792248 title "The effect of temperature acclimation upon succinic dehydrogenase activity from the epaxial muscle of the common goldfish (Carassius auratus L.)—II. Lipid reactivation of the soluble enzyme" @default.
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- W2000792248 doi "https://doi.org/10.1016/0305-0491(72)90231-3" @default.
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