Properties of purifed quinonoid dihydropterin reductase.
Properties of purifed quinonoid dihydropterin reductase.
复制标题
纯化的醌类二氢蝶呤还原酶的性质。
DOI：
10.1139/o73-163
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发表时间：
1973
期刊：
影响因子：
--
通讯作者：
K. Scrimgeour
中科院分区：
文献类型：
--
作者：
S. Cheema;S. Soldin;A. Knapp;K. Hofmann;K. Scrimgeour
从绵羊肝脏、绵羊脑和牛肉肾上腺髓质中提纯了奎诺酮类二氢蝶呤还原酶。这些酶中的每一种都有大约45 000-55 000的分子量，并由两个亚基组成，重量减半。绵羊肝脏还原酶的亚基具有相同的电荷、大小和N-末端氨基酸残基。还原酶以二聚体的形式存在于溶液中，存在的浓度范围很广。由二甲基硫酰亚胺共价连接的二聚体保持了全部活性。报道了喹酮类二氢蝶呤还原酶的一些动力学性质，包括被硫醇试剂和蝶呤类似物抑制。
Quinonoid dihydropterin reductase has been purified to homogeneity from sheep liver, sheep brain, and beef adrenal medulla. Each of these enzymes has a molecular weight of about 45 000–55 000, and is composed of two subunits of half that weight. The subunits of the sheep liver reductase have identical charge, size, and N-terminal amino acid residue. The reductase exists in solution over a wide range of concentrations as the dimer. A dimer covalently linked by dimethylsuberimidate retains full activity. A number of kinetic properties of quinonoid dihydropterin reductase, including inhibition by thiol reagents and by pterin analogues, are reported.