HIGHLY PURIFIED MICROSOMAL P-450 - OXYFERRO INTERMEDIATE STABILIZED AT LOW-TEMPERATURE
HIGHLY PURIFIED MICROSOMAL P-450 - OXYFERRO INTERMEDIATE STABILIZED AT LOW-TEMPERATURE
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DOI：
10.1016/0006-291x(79)91122-7
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发表时间：
1979-01-01
影响因子：
3.1
通讯作者：
MAUREL, P
中科院分区：
文献类型：
--
作者：
BONFILS, C;DEBEY, P;MAUREL, P
从大鼠肝脏中形成高度纯化的微粒体细胞色素P-450的氧化铁中间体，并在-30 ℃下稳定。C在水性缓冲液和甘油（1/1）的混合物中。绝对值和差值。**图形 **。该中间体的光谱似乎与在稳态动力学或停止流动条件下对相同细胞色素以及细菌P-450 cam获得的光谱非常相似。（绝对光谱和差光谱分别在420和557-558 nm处呈现最大值，在442 nm处呈现宽最大值）。随着温度升高，氧铁中间体自动氧化，三价铁P-450恢复。该反应似乎遵循双相一级动力学。两相的速率常数随温度的升高而减小，随质子浓度的升高而增大。
The oxyferro intermediate of highly purified microsomal cytochrome P-450 from rat liver was formed and stabilized at -30.degree. C in a mixture of aqueous buffer and glycerol (1/1). Absolute and difference .**GRAPHIC**. spectra of this intermediate appear to be very similar to those obtained under either steady state kinetics or stopped flow conditions on the same cytochrome as well as on bacterial P-450cam. (Absolute and difference spectra present maxima at 420 and 557-558 nm and a broad maximum at 442 nm, respectively). As temperature increases the oxyferro intermediate autoxidizes and ferric P-450 is restored. This reaction appears to follow biphasic first order kinetics. The rate constant of both phases decreases with temperature and increased with protons concentrations.