Skrzypek-Osiecka I, Robin Y, Porembska Z
Acta Biochim Pol. 1983;30(1):83-92.
Arginase A1 and arginase A4 were isolated from rat kidney. Arginase A4, which is the main form of arginase in rat kidney, was obtained at a highly purified preparation; its specific activity was 1057 mumoles ornithine . min-1 . mg-1 protein. The two forms differed in subcellular localization. Form A1 was restricted to the cytosol while form A4 occurred mainly in the mitochondrial matrix. Kidney arginases A1 and A4 were found to differ in immunological properties. Kidney arginase A1, in contrast to arginase A4, precipitated with antibodies against arginase A1 from rat liver. Arginase A1 from kidney was shown to differ from arginase A1 from the liver. The two enzymes could be distinguished by double diffusion test and immunoelectrophoresis.
精氨酸酶A1和精氨酸酶A4是从大鼠肾脏中分离出来的。精氨酸酶A4是大鼠肾脏中精氨酸酶的主要形式,通过高度纯化制备获得;其比活性为1057微摩尔鸟氨酸·分钟⁻¹·毫克⁻¹蛋白质。这两种形式在亚细胞定位上有所不同。形式A1局限于细胞质溶胶,而形式A4主要存在于线粒体基质中。发现肾脏精氨酸酶A1和A4在免疫特性上存在差异。与精氨酸酶A4相比,肾脏精氨酸酶A1能与抗大鼠肝脏精氨酸酶A1的抗体沉淀。已证明肾脏中的精氨酸酶A1与肝脏中的精氨酸酶A1不同。这两种酶可以通过双向扩散试验和免疫电泳加以区分。