Ryle C M, Tipton K F
Biochem J. 1981 Sep 1;197(3):715-20. doi: 10.1042/bj1970715.
The distribution of the two principal isoenzymes of aldehyde reductase (EC 1.1.1.2) has been studied in ox brain. The more active of these, which has been termed the high-Km enzyme, has been shown to be located in the cytosol and the less abundant low-Km form has a similar localization. p-Nitrobenzaldehyde, which has been used as a substrate in previous studies, caused the reduction of NADH in the presence of the mitochondrial fraction, but mixed substrate experiments with 1,3-dinitrobenzene and the effects of pH on the activity indicate that this is due to the presence of a nitro reductase activity which has been recently described (Köchli, Wermuth & von Wartburg (1980) Biochim. Biophys. Acta 616, 133-142] rather than to the low-Km aldehyde reductase activity. Fractionation of the mitochondria indicated this activity to be largely confined to the mitochondrial inner membrane.
已对牛脑中醛还原酶(EC 1.1.1.2)的两种主要同工酶的分布进行了研究。其中活性较高的那种,被称为高Km酶,已被证明位于胞质溶胶中,而含量较少的低Km形式也有类似的定位。在先前的研究中用作底物的对硝基苯甲醛,在线粒体部分存在的情况下会导致NADH的还原,但用1,3 -二硝基苯进行的混合底物实验以及pH对活性的影响表明,这是由于最近描述的硝基还原酶活性的存在[Köchli, Wermuth & von Wartburg (1980) Biochim. Biophys. Acta 616, 133 - 142],而非低Km醛还原酶活性。线粒体分级分离表明这种活性主要局限于线粒体内膜。