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- W2062669796 abstract "Previous studies in our laboratory have indicated that polyphenol oxidase (PPO), as measured by its activity, is not present in tentoxin-treated plants. In the present study, immunochemical techniques were used as a sensitive probe of tentoxin effects on PPO. Immunocytochemistry of PPO with peroxidase-antiperoxidase labelling techniques, revealed that in control Vicia faba L. chloroplasts, PPO was associated mainly with the thylakoids. Cytochemical staining of PPO activity using DL-dihydroxyphenylalanine (DOPA) as substrate was also localized only on the thylakoids in the control chloroplasts. In tentoxin-treated plants all of the immunologically-recognizable PPO accumulated at the plastid envelope although no PPO was detected by cytochemical methods. SDS polyacrylamide gels of extracts from control and tentoxin-treated Vicia leaves were blotted onto nitrocellulose and reacted with rabbit anti-PPO. Secondary labelling of the blots with goat-antirabbit IgG labelled with peroxidase revealed a 40 kdalton protein in both extracts. However, only the PPO from the control extract had DOPA oxidase activity. These data suggest that PPO accumulates in the plastid envelope membranes in tentoxin-affected cells and that PPO in these treated plants is not processed to an active protein." @default.
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- W2062669796 date "1984-02-01" @default.
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- W2062669796 title "Tentoxin stops the processing of polyphenol oxidase into an active protein" @default.
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- W2062669796 doi "https://doi.org/10.1111/j.1399-3054.1984.tb04574.x" @default.
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