[大鼠肝脏泛酸激酶的纯化及各种性质]
[Purification and various properties of pantothenate kinase from the rat liver].
作者信息
Khomich T I, Moiseenok A G, Voskoboev A I
出版信息
Biokhimiia. 1990 Aug;55(8):1468-73.
Homogeneous (according to disc gel electrophoresis data) ATP: D-pantothenate-4'-phosphotransferase (pantothenate kinase, EC 2.7.1.33) was obtained from rat liver cytosol of heterogeneous stock rats. The enzyme was purified 199-fold with a 9.3% yield. The enzyme was relatively unstable but retained its activity in the presence of 10% glycerol containing 5.10(-4) M ATP over 10 days at 4 degrees C. The pH optimum was 6.5; the apparent Km values were equal to 1.2 X 10(-5) M and 1.4 X 10(-3) M for pantothenate and ATP, respectively, at the ATP/Mg2+ ratio of 1. Pantetheine produced a competitive inhibition of pantothenate kinase. Pantethine or pantetheine disulfide did not inhibit the enzyme.
（根据圆盘凝胶电泳数据）从杂种大鼠的大鼠肝脏胞质溶胶中获得了均一的ATP：D - 泛酸盐 - 4'-磷酸转移酶（泛酸盐激酶，EC 2.7.1.33）。该酶纯化了199倍，产率为9.3%。该酶相对不稳定，但在含有5×10⁻⁴ M ATP的10%甘油存在下，于4℃可保持活性超过10天。最适pH为6.5；在ATP/Mg²⁺ 比例为1时，泛酸盐和ATP的表观Km值分别等于1.2×10⁻⁵ M和1.4×10⁻³ M。泛硫乙胺对泛酸盐激酶产生竞争性抑制作用。泛硫辛或泛硫乙胺二硫化物不抑制该酶。
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