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Inactivation and Protection of Fructose Diphosphate Aldolase in Rat Adipose Tissue Extracts

From the ¹ From the Department of Biochemistry, the Hebrew University Hadassah Medical School, Jerusalem, Israel

Previous estimates of rat adipose tissue aldolase, which were too low to account for the magnitude of lipogenesis from glucose, were found to be due to instability of the enzyme during the isolation. The addition of inorganic phosphate or various phosphorylated glycolytic intermediates during homogenization of rat adipose tissue increased the activity of fructose-1,6-diphosphate aldolase 3- to 5-fold. Partial protection was obtained also by the addittion of 0.5 m NaCl, 0.154 m KCl, or 0.1 m NaF. Adipose tissue slices previously incubated with inorganic phosphate show high aldolase activity even when homogenized in the absence of added phosphate. Sodium oleate inhibited aldolase activity in extracts obtained from rat adipose tissue.

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