MONOAMINE OXIDASE CATALYZED DEGRADATION OF PHENELZINE-1-14C AN IRREVERSIBLE INHIBITOR OF MONOAMINE OXIDASE .2.
MONOAMINE OXIDASE CATALYZED DEGRADATION OF PHENELZINE-1-14C AN IRREVERSIBLE INHIBITOR OF MONOAMINE OXIDASE .2.
复制标题
DOI：
10.1016/0006-2952(69)90104-x
复制
发表时间：
1969-01-01
影响因子：
5.8
通讯作者：
HORITA, A
中科院分区：
文献类型：
--
作者：
CLINESCHMIDT, BV;HORITA, A
苯乙肼-1-14 C在大鼠肝匀浆线粒体生物转化系统中的转化产物，其薄层色谱特征与苯乙酸-1-14 C的特征完全一致。（2）依赖于O2的存在;（3）通过煮沸消除系统的线粒体组分;和（4）通过用异羧酰肼，非尼哌嗪，这些结果为单胺氧化酶（MAO）的不可逆抑制剂提供了第一个实质性证据。作为酶的底物，结果表明，抑制剂的降解很可能是通过氧化脱水完成的，这是一种以前对MAO未知的反应机制。
Exposure of phenelzine-1-14C to a biotransformation system which included mitochondria isolated from homogenate of rat liver resulted in a metabolite with thinlayer Chromatographic characteristics identical to those of authentic phenylacetic-1-14C acid.The conversion of phenelzine to phenylacetic acid was found to be: (1) relatively insensitive to preincubation of the bioconversion system with cyanide; (2) dependent upon the presence of O2; (3) abolishing by boiling the mitochondrial component of the system; and (4) inhibited by preincubation of the biotransformation system with isocarboxazid, pheniprazine, tranylcypromine or pargyline.These results provide the first substantial evidence for an irreversible inhibitor of monoamine oxidase (MAO) acting as a substrate of the enzyme, and the results suggest that degradation of the inhibitor is very likely accomplished by oxidative dehydrazination, a reaction mechanism previously unknown for MAO.