Abstract
Peroxidase activity in extracts of adult female Meloidogyne incognita was influenced by the host plant on which the nematode was propagated. Extracts of nematodes propagated on tobacco contained only 56% as much peroxidase activity as extracts from nematodes propagated on tomato. Two peroxidase isoenzymes separated by polyacrylamide-gel electrophoresis from extracts of adult female nematodes propagated on tomato had the capacity to oxidize several aromatic amines and phenols. A positive reaction for peroxidase in stylet exudates of adult female nematodes was obtained cytochemically with o-dianisidine in the presence of hydrogen peroxide. This reaction was inhibited by 5 m m-potassium cyanide.
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