Reconstitution of the ribonucleotide reductase enzyme from Ehrlich tumor cells.
Reconstitution of the ribonucleotide reductase enzyme from Ehrlich tumor cells.
复制标题
从艾利希肿瘤细胞中重建核糖核苷酸还原酶。
DOI：
10.1016/s0021-9258(17)40778-2
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发表时间：
1978
期刊：
影响因子：
--
通讯作者：
J. Munro
中科院分区：
文献类型：
--
作者：
J. G. Cory;A. E. Fleischer;J. Munro
通过蓝色葡聚糖/琼脂糖凝胶层析将来自埃利希肿瘤细胞的核糖核苷酸还原酶分离成两个蛋白级分（Tris和Dye级分）。两个馏分单独具有还原酶活性，但当组合时，构成了活性酶系统。热处理的任一馏分导致在一个非活性的组合。与完整酶的9 S相比，确定Tris和染料级分的活性组分的近似分子大小分别为5.7 S和6.5 S。通过羟胺使Tris级分失活，而通过磷酸吡哆醛/BH 4处理使染料级分失活。ATP可阻止染料组分的失活。这些数据将表明，Tris和染料级分在功能上分别与大肠杆菌核糖核苷酸还原酶的B2和B1蛋白相当。
Ribonucleotide reductase from Ehrlich tumor cells was separated by chromatography on blue dextran/Sepharose into two protein fractions (Tris and Dye fractions). Neither fraction alone had reductase activity, but when combined, constituted an active enzyme system. Heat treatment of either fraction resulted in an inactive combination. The approximate molecular size of the active component of the Tris and Dye fractions was determined to be 5.7 S and 6.5 S, respectively, compared to 9 S for the intact enzyme. The Tris fraction was inactivated by hydroxylamine while the dye fraction was inactivated by pyridoxal phosphate/BH4-treatment. The inactivation of the Dye fraction was prevented by ATP. These data would indicate that the Tris and Dye fractions were comparable in function to the B2 and B1 proteins, respectively, of the Escherichia coli ribonucleotide reductase.