PURIFICATION OF CYTOCHROME-P-450D1-ALPHA (25-HYDROXYVITAMIN-D3-1-ALPHA-HYDROXYLASE) OF BOVINE KIDNEY MITOCHONDRIA
PURIFICATION OF CYTOCHROME-P-450D1-ALPHA (25-HYDROXYVITAMIN-D3-1-ALPHA-HYDROXYLASE) OF BOVINE KIDNEY MITOCHONDRIA
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DOI：
10.1016/s0006-291x(82)80047-8
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发表时间：
1982-01-01
影响因子：
3.1
通讯作者：
ICHIKAWA, Y
中科院分区：
文献类型：
--
作者：
HIWATASHI, A;NISHII, Y;ICHIKAWA, Y
细胞色素P-450 D1 α。从牛肾线粒体中纯化的蛋白质在电泳上是均匀的，并且给出单一的蛋白质带。细胞色素P-450 D1 α。具有与其他组织的线粒体细胞色素P-450共同的免疫化学加工特性。1.阿尔法用细胞色素P-450 D1 α重建25-羟基维生素D3的羟化酶系统，NADPH-肾氧还蛋白还原酶和肾氧还蛋白，每种组分对于1 α-还原酶和1 α-还原酶都是必需的。羟化酶系统细胞色素P-450 D1 α的底物特异性被查
Cytochrome P-450D1.alpha. purified from bovine renal mitochondria was electrophoretically homogeneous and gave a single protein band. The cytochrome P-450D1.alpha. has immunochemical processing properties in common with the mitochondrial cytochrome P-450 of other tissues. The 1.alpha.-hydroxylase system of 25-hydroxyvitamin D3 was reconstituted with the cytochrome P-450D1.alpha., NADPH-renoredoxin reductase and renoredoxin, each component being essential to the 1.alpha.-hydroxylase system. The substrate specificity of the cytochrome P-450D1.alpha. was investigated.