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Plant Physiology 63:93-99 (1979)
© 1979 American Society of Plant Biologists

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Articles

Tomato Peroxidase

Purification, Characterization, and Catalytic Properties 1

Demetri M. Kokkinakis2 and James L. Brooks

a Plant Science Division, College of Agriculture and Forestry, West Virginia University, Morgantown, West Virginia 26506

A major peroxidase has been found in the tomato pericarp (Lycopersicon esculentum var. Tropic) of the ripe and green fruit. A purification scheme yielding this enzyme approximately 85% pure has been developed. The tomato enzyme resembles horseradish peroxidase (HRP) in a standard peroxidase assay and in its ability to be reduced to ferroperoxidase, to be converted to oxyferroperoxidase (compound III), and to form peroxidase complexes with hydrogen peroxide (compounds I and II). In contrast to the HRP, the tomato peroxidase fails to catalyze the aerobic oxidation of indole-3-acetic acid in the presence of 2,4-dichlorophenol and manganese. The tomato peroxidase can be resolved into two nonidentical subunits in the presence of dithiothreitol while HRP remains as a single polypeptide chain after such treatment. Dithiothreitol is oxidized in the presence of tomato or horseradish peroxidase with the enzymes accumulating in their oxyferroperoxidase forms during the oxidation reaction. Whereas HRP returns to its free ferric form at the end of the reaction, the tomato enzyme is converted into a form that absorbs at 442 nanometers.

2 Present address: Texas Tech University School of Medicine, Department of Biochemistry, P.O. Box 4569, Lubbock, Texas 79409.

1 Published with the approval of the Director of the West Virginia Agriculture and Forestry Experiment Station as Scientific Paper No. 1533.






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Copyright © 1979 by the American Society of Plant Biologists