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- W2024725061 abstract "1. Aldolase activity of a rabbit-liver preparation against fructose 1,6-diphosphate and fructose 1-phosphate could not be separated by heat-inactivation procedures performed at pH values varying from 4.5 to 10.4, which supports the theory that these two activities are exerted by the same enzyme. 2. Under certain conditions of assay, the removal of triose-phosphate isomerase (d-glyceraldehyde-3-phosphate ketol-isomerase, EC 5.3.1.1) activity strongly decreased the apparent aldolase activity against fructose 1,6-diphosphate but did not affect the activity against fructose 1-phosphate. The activity against fructose 1,6-diphosphate was restored by the addition of triose-phosphate isomerase. 3. The apparent purification of liver fructose-1-phosphate aldolase activity from fructose-1,6-diphosphate aldolase earlier described by other authors, seems possible to explain as an artifact, caused by the separation of the aldolase from triose-phosphate isomerase." @default.
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- W2024725061 date "1964-04-01" @default.
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- W2024725061 title "The influence of the method of assay on the apparent specificity of rabbit-liver aldolase" @default.
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- W2024725061 doi "https://doi.org/10.1016/0926-6569(64)90173-7" @default.
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