Kaysen G A, Strecker H J
Biochem J. 1973 Aug;133(4):779-88. doi: 10.1042/bj1330779.
l-Arginase from rat kidney was partially purified and some properties were compared with those of l-arginase of rat liver. The kidney enzyme was firmly bound to the mitochondrial fraction and after solubilization required arginine or an unknown factor in tissue extracts for stabilization after dialysis. The two enzymes differed also in stability with respect to acetone treatment, heating or freezing. In further contrast with liver arginase, arginase from kidney was not adsorbed to CM-cellulose at pH7.5 and its activity was not increased by incubation with Mn(2+). Other differences were seen in relative specificities for substrates, ratio of hydrolysis rates with high and low concentrations of arginine and effects of certain inhibitors. Antisera prepared to pure liver arginase did not cross-react with partially purified kidney arginase.
对大鼠肾脏中的L-精氨酸酶进行了部分纯化,并将其一些特性与大鼠肝脏的L-精氨酸酶进行了比较。肾脏中的这种酶与线粒体部分紧密结合,溶解后在透析后需要精氨酸或组织提取物中的一种未知因子来稳定。这两种酶在丙酮处理、加热或冷冻方面的稳定性也有所不同。与肝脏精氨酸酶进一步不同的是,肾脏中的精氨酸酶在pH7.5时不吸附到CM-纤维素上,并且与Mn(2+)一起孵育时其活性不会增加。在底物的相对特异性、高浓度和低浓度精氨酸的水解速率比以及某些抑制剂的作用方面也存在其他差异。针对纯肝脏精氨酸酶制备的抗血清与部分纯化的肾脏精氨酸酶不发生交叉反应。