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• W2029536124 abstract "Enolase has been purified approximately 60–70-fold from both young and old Turbatrix aceti (nematodes). Both preparations are homogeneous as shown by gel electrophoresis, immunodiffusion and other criteria. The “old” enolase has a sharply reduced specific activity both in crude homogenates and in the pure preparation, compared to the “young” enzyme. The “old” enzyme is also much more sensitive to heat as shown by heat-stability determinations. At 52.5 °C, a biphasic pattern is obtained with a rapidly deteriorating component amounting to 40% of the enzyme. The remaining activity depreciates more slowly but more rapidly than the rate of loss of “young” enzyme activity. The results support the idea that “old” enzyme consists of active and partially active molecules, or perhaps entirely of the latter, rather than a mixture of active and inactive molecules. Molecular weight (82,000), subunit size (41,000), absence of isozymes, Km, Ki (phosphate), index of fluoride inhibition and net charge (gel electrophoresis) are the same for both preparations. Enolase from T. aceti has been compared with enolase from other sources. The nematode enzyme is similar to the rabbit enzyme with regard to molecular weight, subunits and index of fluoride inhibition but differs in charge and pH optimum." @default.
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• W2029536124 date "1976-05-01" @default.
• W2029536124 modified "2023-10-16" @default.
• W2029536124 title "Age-related alteration of enolase in the free-living nematode, Turbatrix aceti" @default.
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• W2029536124 doi "https://doi.org/10.1016/0003-9861(76)90351-9" @default.
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