Pakyrbaéva L V, Shushevich S I, Khalmuradov A H, Chahovets' R V
Ukr Biokhim Zh. 1975 Jan-Feb;47(1):3-7.
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.
对大鼠肝细胞核NAD - 糖水解酶(EC 3.2.2.5)的某些特性进行了研究。已确定其最高活性出现在37摄氏度,活化能等于9480卡/摩尔,Q10因子等于1.5。该酶在0.2M醋酸三羟甲基氨基甲烷中的最适pH值为6.5,在0.2M磷酸钾中为7.5。结果表明,该酶仅对β - NAD表现出严格的特异性,几乎不分解NADP,且不影响NADH、NADPH和NMN。确定了该酶对NAD的表观Km值。异烟肼、烟酰胺以及程度较轻的烟酸会抑制细胞核的酶活性。乙二胺四乙酸(EDTA)、乙二醇双乙醚二胺四乙酸(EGTA)、对氯汞苯甲酸(p - CMB)、巯基乙醇不会引起大鼠肝细胞核对NAD酶活性的任何变化。