Purification and properties of alpha-aminoadipate aminotransferase from rat liver and kidney mitochondria.

M R Mawal, A Mukhopadhyay, D R Deshmukh
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引用次数: 5

Abstract

Recently we reported an affinity chromatography method to purify alpha-aminoadipate aminotransferase (AadAT) activity from rat kidney supernatant fraction. Using the same affinity column, we purified AadAT activities from rat kidney and liver mitochondria. The physical and kinetic properties such as pH optima, Km for substrates, molecular weight, subunit structure, isoelectric pH, electrophoretic mobility and inhibition by dicarboxylic acids of mitochondrial AadAT were similar to those of the AadAT from rat kidney supernatant fraction. These results indicate that AadAT from different subcellular fractions is structurally and immunologically identical.

大鼠肝、肾线粒体α -氨基己二酸转氨酶的纯化及性质研究。
最近,我们报道了一种亲和层析法从大鼠肾上清中纯化α -氨基己二酸氨基转移酶(AadAT)活性。使用相同的亲和柱,我们从大鼠肾脏和肝脏线粒体中纯化了AadAT活性。线粒体AadAT的最优pH值、底物Km、分子量、亚基结构、等电pH值、电泳迁移率和对二羧酸的抑制作用等物理和动力学性质与大鼠肾上清部分的AadAT相似。这些结果表明,不同亚细胞组分的AadAT在结构和免疫学上是相同的。
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