[Properties of NAD-glycohydrolase of the nuclei of the liver cells of rats].
Certain properties of the rat liver cell nuclei NAD-glycohydrolase (EC 3.2.2.5) were investigated. It is established that its highest activity is at 37 degrees with activation energy equal to 9480 cal/M and with factor Q10 equal to 1.5. The enzyme pH optimum in 0.2 M tris acetate is equal to 6.5 and in 0.2 potassium phosphate - 7.5. It was shown that the enzyme manifests its strict specificity only with beta-NAD, and it hardly decomposes NADP without affecting NADH, NADPH and NMN. The apparent Km value of the enzyme with respect to NAD is established. Isonicotinic acid hydrazide, nicotinamide and to the less extent nicotinic acid inhibit the enzymatic activity of nuclei. EDTA, EGTA, p-CMB, mercaptoethanol do not cause any changes in the rat liver cells nuclei NADase activity.
[Properties of NAD-glycohydrolase of the nuclei of the liver cells of rats]. Certain properties of the rat liver cell nuclei NAD-glycohydrolase (EC 3.2.2.5) were investigated. It is established that its highest activity is at 37 degrees with activation energy equal to 9480 cal/M and with factor Q10 equal to 1.5. The enzyme pH optimum in 0.2 M tris acetate is equal to 6.5 and in 0.2 potassium phosphate - 7.5. It was shown that the enzyme manifests its strict specificity only with beta-NAD, and it hardly decomposes NADP without affecting NADH, NADPH and NMN. The apparent Km value of the enzyme with respect to NAD is established. Isonicotinic acid hydrazide, nicotinamide and to the less extent nicotinic acid inhibit the enzymatic activity of nuclei. EDTA, EGTA, p-CMB, mercaptoethanol do not cause any changes in the rat liver cells nuclei NADase activity.