Jauniaux J C, Urrestarazu L A, Wiame J M
J Bacteriol. 1978 Mar;133(3):1096-1107. doi: 10.1128/jb.133.3.1096-1107.1978.
Subcellular localization of enzymes of arginine metabolism in Saccharomyces cerevisiae was studied by partial fractionation and stepwise homogenization of spheroplast lysates. These enzymes could clearly be divided into two groups. The first group comprised the five enzymes of the acetylated compound cycle, i.e., acetylglutamate synthase, acetylglutamate kinase, acetylglutamyl-phosphate reductase, acetylornithine aminotransferase, and acetylornithine-glutamate acetyltransferase. These enzymes were exclusively particulate. Comparison with citrate synthase and cytochrome oxidase, and results from isopycnic gradient analysis, suggested that these enzymes were associated with the mitochondria. By contrast, enzymatic activities going from ornithine to arginine, i.e., arginine pathway-specific carbamoylphosphate synthetase, ornithine carbamoyltransferase, argininosuccinate synthetase, and argininosuccinate lyase, and the two first catabolic enzymes, arginase and ornithine aminotransferase, were in the "soluble" fraction of the cell.
通过对球状体裂解物进行部分分级分离和逐步匀浆，研究了酿酒酵母中精氨酸代谢酶的亚细胞定位。这些酶可明显分为两组。第一组包括乙酰化化合物循环的五种酶，即乙酰谷氨酸合酶、乙酰谷氨酸激酶、乙酰谷氨酰磷酸还原酶、乙酰鸟氨酸氨基转移酶和乙酰鸟氨酸-谷氨酸乙酰转移酶。这些酶仅存在于颗粒部分。与柠檬酸合酶和细胞色素氧化酶的比较以及等密度梯度分析的结果表明，这些酶与线粒体相关。相比之下，从鸟氨酸到精氨酸的酶活性，即精氨酸途径特异性氨甲酰磷酸合成酶、鸟氨酸氨甲酰转移酶、精氨琥珀酸合成酶和精氨琥珀酸裂解酶，以及最初的两种分解代谢酶，精氨酸酶和鸟氨酸氨基转移酶，存在于细胞的“可溶性”部分。
