Traniello S, Barsacchi R, Magri E, Grazi E
Biochem J. 1975 Feb;145(2):153-7. doi: 10.1042/bj1450153.
Chicken kidney contains two arginases with different sedimentation coefficients and substrate specificity. The ligher of these arginases, which hydrolyses only L-arginine, has been purified about 3000-fold. Like the "ureotelic" arginase, developed in chicken liver after starvation, it displays many of the properties of the arginase of the "ureotelic" species. This seems to exclude the possibility that ureotelism and uricotelism are characterized by a specific type of arginases. Both liver and kidney arginases are located in the mitochondrial matrix. The rate of hydrolysis of arginine thus not only depends on the arginase activity but also on the rate of transport of arginine into the matrix. This last process therefore is of regulatory significance.
鸡肾含有两种沉降系数和底物特异性不同的精氨酸酶。其中较轻的那种精氨酸酶仅水解L-精氨酸,已被纯化了约3000倍。与饥饿后鸡肝脏中产生的“排尿素型”精氨酸酶一样,它具有“排尿素型”物种精氨酸酶的许多特性。这似乎排除了排尿素代谢和排尿酸代谢以特定类型精氨酸酶为特征的可能性。肝脏和肾脏中的精氨酸酶都位于线粒体基质中。因此,精氨酸的水解速率不仅取决于精氨酸酶的活性,还取决于精氨酸向基质的转运速率。所以最后这个过程具有调节意义。