Purification of mixed-function amine oxidase from rat liver microsomes.
Purification of mixed-function amine oxidase from rat liver microsomes.
复制标题
从大鼠肝微粒体中纯化混合功能胺氧化酶。
DOI：
10.1016/0006-291x(83)91197-x
复制
发表时间：
1983
影响因子：
3.1
通讯作者：
C. Nagata
中科院分区：
文献类型：
--
作者：
T. Kimura;M. Kodama;C. Nagata
To clarify the metabolism of carcinogenic aminoazo dyes in target tissues, mixed function amine oxidase (MFAO) was purified from rat liver. The MFAO was solubilized from microsomes with Triton X in the presence of 20% glycerol and 1 mM EDTA and purified successively with DEAE Sepharose CL-6B, 2′,5′-ADP Sepharose 4B and Hydroxyapatite column chromatography. The purified enzyme yielded a single protein band on sodium dodecyl sulfate (SDS)-poly-acrylamide gel electrophoresis. The apparent molecular weight was about 59,000. When dimethylaniline (DMA) was used as a substrate, the specific activity of the enzyme fortified with NADPH was about 430 nmol DMA N-oxide formed/mg protein/min with a yield of about 15%. N-Demethylation of dimethyl-aminoazobenzene (DAB) with the enzyme proceeded only when iron was added to the reaction system.
细胞色素 P-450 同工酶在大鼠 N,N-二甲基-4-氨基偶氮苯代谢中的作用。
DOI：
--
发表时间：
1982
期刊：
Drug metabolism and disposition: the biological fate of chemicals
影响因子：
--
作者：
Levine,WG;Lu,AY
通讯作者：
Lu,AY