Purification and characterization of a benzene hydroxylase from rat liver mitochondria.
Purification and characterization of a benzene hydroxylase from rat liver mitochondria.
复制标题
大鼠肝线粒体苯羟化酶的纯化和表征。
DOI：
10.1016/0304-4165(90)90121-c
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发表时间：
1990
期刊：
影响因子：
--
通讯作者：
Kalf,GF
中科院分区：
文献类型：
--
作者：
Karaszkiewicz,JW;Kalf,GF
从大鼠肝线粒体中提纯了一种将苯代谢为苯酚的酶。该酶的相对分子质量为52 000，需要NADPH、阿伦多辛和肾上腺素还原酶才能产生活性，一氧化碳和SKF-525A以及苯代谢的特异性抑制剂都能抑制苯羟基酶的活性。纯化后的酶还能将苯酚氧化成邻苯二酚。这些数据表明，微线粒体起源的细胞色素P-450参与了苯代谢，并为线粒体在异种生物激活中的作用提供了另一个例子。
An enzyme has been purified to electrophoretic homogeneity from rat liver mitoplasts which metabolizes benzene to phenol. The enzyme has aMrof 52 000 and requires NADPH, adrendoxin, and adrenodoxin reductase for activity, Benzene hydroxylase activity could be inhibited by carbon monoxide and SKF-525A, and by specific inhibitors of microsomal benzene metabolism. The purified enzyme also oxidized phenol to catechol. The data suggest that a cytochromeP-450 of microchondrial origin is involved in benzene metabolism, and provide another example of a role for the mitochondrion in xenobiotic activation.