Ikegami T, Natsumeda Y, Weber G
Life Sci. 1987 Jun 8;40(23):2277-82. doi: 10.1016/0024-3205(87)90064-6.
IMP dehydrogenase (EC 1.1.1.205), the rate-limiting enzyme of de novo GTP biosynthesis and a promising target for cancer chemotherapy, was purified 4860-fold to homogeneity from rat hepatoma 3924A by a method including affinity chromatography in which IMP is bound to epoxy-activated Sepharose 6B. This affinity gel provided a specific elution of the enzyme with 0.5 mM IMP. The final enzyme preparation gave a single band with a molecular weight of 60,000 +/- 1000 on sodium dodecyl sulfate polyacrylamide gel electrophoresis.
肌苷酸脱氢酶(EC 1.1.1.205)是从头合成GTP的限速酶,也是癌症化疗的一个有前景的靶点,通过一种包括亲和层析的方法从大鼠肝癌3924A中纯化了4860倍至同质,该方法中肌苷酸与环氧活化的琼脂糖凝胶6B结合。这种亲和凝胶用0.5 mM肌苷酸对该酶进行特异性洗脱。最终的酶制剂在十二烷基硫酸钠聚丙烯酰胺凝胶电泳上呈现出一条分子量为60,000±1000的单一谱带。