Department of Biochemistry and Microbiology, Cook College, Rutgers-The State University of New Jersey, New Brunswick, New Jersey 08903.
Plant Physiol. 1983 May;72(1):80-5. doi: 10.1104/pp.72.1.80.
The intracellular localization of aryl acylamidase (aryl-acylamide amidohydrolase, EC 3.5.1.13) in rice (Oryza sativa L. var Starbonnet) leaves was investigated. The enzyme hydrolyzes and detoxifies the herbicide propanil (3,4-dichloropropionanilide) thereby accounting for immunity of the rice plant to herbicidal action. Fractionation of mesophyll protoplasts by differential centrifugation yielded the highest specific activity of amidase in the crude mitochondrial fraction. Further separation of density gradients of the silica sol Percoll also indicated that this enzyme was mitochondrial. By the use of biochemical markers, the purified mitochondrial fraction was shown to be substantially free of contamination from nuclei, chloroplasts, golgi, and plasma membranes. Subfractionation of the purified mitochondria suggests that this enzyme is located on the outer membrane.
研究了水稻（Oryza sativa L. var Starbonnet）叶片中芳基酰基酰胺酶（芳基-酰基酰胺 amidohydrolase，EC 3.5.1.13）的细胞内定位。该酶水解并解毒除草剂丙草胺（3,4-二氯丙酰替苯胺），从而使水稻植株对除草剂的作用具有免疫力。差速离心分离叶肉原生质体可获得粗线粒体部分中酰胺酶的最高比活性。硅胶溶胶 Percoll 密度梯度的进一步分离也表明该酶是线粒体的。通过生化标记物，纯化的线粒体部分显示出基本上不含核、叶绿体、高尔基体和质膜的污染。纯化线粒体的亚组分分离表明该酶位于外膜上。
