Plant Physiol. Drug Metab Dispos
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Plant Physiology 72:80-85 (1983)
© 1983 American Society of Plant Biologists

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Articles

Subcellular Localization of Rice Leaf Aryl Acylamidase Activity 1

John J. Gaynor2 and Cecil C. Still3

Department of Biochemistry and Microbiology, Cook College, Rutgers—The State University of New Jersey, New Brunswick, New Jersey 08903

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.

2 In partial fulfillment of the PhD degree, Rutgers University. Present address: Laboratory of Plant Molecular Biology, Rockefeller University, New York, NY 10021.

3 To whom reprint requests should be addressed.

1 This work is New Jersey Agricultural Experiment Station Publication No. D-01201-1-82, supported by State Funds and by the U. S. Hatch Act.






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Copyright © 1983 by the American Society of Plant Biologists