草分枝杆菌二氢叶酸还原酶的纯化及特性研究
Purification and characterization of dihydrofolate reductase from Mycobacterium phlei.
作者信息
Al-Rubeai M, Dale J W
出版信息
Biochem J. 1986 Apr 1;235(1):301-3. doi: 10.1042/bj2350301.
Abstract
The dihydrofolate reductase from Mycobacterium phlei was purified and characterized; it has an Mr of 15 000 and a pI of 4.8. It is competitively inhibited by both methotrexate and trimethoprim, although the affinity is less than for other bacterial dihydrofolate reductases.
摘要
纯化并鉴定了草分枝杆菌的二氢叶酸还原酶；其相对分子质量为15000，等电点为4.8。甲氨蝶呤和甲氧苄啶对其均有竞争性抑制作用，尽管其亲和力低于其他细菌的二氢叶酸还原酶。
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