Subcellular distribution and properties of rabbit liver aldehyde dehydrogenases.
Subcellular distribution and properties of rabbit liver aldehyde dehydrogenases.
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兔肝醛脱氢酶的亚细胞分布和特性。
DOI：
10.1016/0006-2952(81)90628-6
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发表时间：
1981
影响因子：
5.8
通讯作者：
Lindahl,R
中科院分区：
文献类型：
--
作者：
Lindahl,R
在兔肝中，鉴定了NAD+和NADP+依赖性乙醛脱氢酶。活性分布在至少三个主要组的同工酶可通过凝胶电泳。这些同工酶也不同的底物和辅酶的喜好，亚细胞分布，和/或效应。NAD+依赖的醛脱氢酶活性分布在线粒体，微粒体和胞质组分。NADP+依赖性醛脱氢酶活性主要是微粒体的，几乎没有真正的胞质NADP+依赖性活性可证明。在所有三个馏分中，脂肪醛被醛脱氢酶氧化得同样好。然而，芳香醛优先被微粒体醛脱氢酶氧化。双硫仑显著抑制线粒体（45%）和胞质（93%）NAD+依赖性醛脱氢酶，但不会显著抑制微粒体NAD+依赖性活性。双硫仑在所有亚细胞组分中抑制NADP+依赖性醛脱氢酶活性（> 71%）。己烯雌酚激活线粒体和细胞质中NAD+和NADP+依赖的乙醛脱氢酶。微粒体乙醛脱氢酶不受己烯雌酚的影响。
In rabbit liver, both NAD+- and NADP+-dependent aldehyde dehydrogenases were identified. The activities were distributed among at least three major groups of isozymes identifiable by gel electrophoresis. These isozymes also differed in their substrate and coenzyme preferences, subcellular distributions, and/or responses to effectors. The NAD+-dependent aldehyde dehydrogenase activity was distributed among the mitochondrial, microsomal, and cytosolic fractions. The NADP+-dependent aldehyde dehydrogenase activity was largely microsomal, with little true cytosolic NADP+-dependent activity demonstrable. Aliphatic aldehydes were oxidized equally well by aldehyde dehydrogenases in all three fractions. Aromatic aldehydes, however, were preferentially oxidized by microsomal aldehyde dehydrogenases. Disulfiram significantly inhibited mitochondrial (45 per cent) and cytosolic (93 per cent) NAD+-dependent aldehyde dehydrogenase, but it did not cause significant inhibition of microsomal NAD+-dependent activity. Disulfiram inhibited the NADP+-dependent aldehyde dehydrogenase activity (>71 per cent) in all subcellular fractions. Diethylstilbestrol activated both NAD+- and NADP+-dependent aldehyde dehydrogenases in mitochondria and cytosol. Microsomal aldehyde dehydrogenases were not affected by diethylstilbestrol.