Suman Mishra, Rajnikant Mishra
Indian J Exp Biol. 2017 Feb;55(2):74-8.
Arginase, that regulates metabolism of arginine, is widely distributed in organisms. The two major isoforms, cytosolic Arginase-I, and mitochondrial Arginase-II have been characterized well. However, reports also suggest another mitochondrial membrane-bound arginase which is extracted by washing the mitochondria with KCl. Here, we studied this mitochondrial membrane-bound arginase among vertebrates. Our observations support that arginase activity is predominant in cytosol which is designated as Arginase-I. The mitochondrial membrane-bound Arginase (mbArg) which resembles Arginase-II seems independent of nitrogen excretion pattern because of its presence both in ureogenic and non-ureogenic vertebrates.
精氨酸酶可调节精氨酸的代谢，广泛分布于生物体内。两种主要的同工型，即胞质型精氨酸酶-I和线粒体型精氨酸酶-II，已得到充分表征。然而，也有报道指出另一种线粒体膜结合精氨酸酶，它可通过用氯化钾洗涤线粒体来提取。在此，我们研究了脊椎动物中的这种线粒体膜结合精氨酸酶。我们的观察结果支持精氨酸酶活性在胞质中占主导地位，这种胞质型精氨酸酶被命名为精氨酸酶-I。线粒体膜结合精氨酸酶（mbArg）与精氨酸酶-II相似，由于其在产尿素和非产尿素的脊椎动物中均有存在，似乎与氮排泄模式无关。
