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- W2031449649 abstract "Three peroxidases which could utilize ascorbate as a reductant were found in roots of Brassica campestris, and designated P I, P II and P III according to their order of elution from a DEAE-Cellulofine chromatography column. P I was not adsorbed to the column and oxidized ascorbate at only 4% of the rate for pyrogallol. Both P II and P III had a high preference for ascorbate as an electron donor and no activity with guaiacol. P II was detected in all tissues of B. campestris, whereas P III was detected characteristically in roots and accounted for 70% of the total ascorbate-peroxidizing activity in 9-day-old roots. Partially purified P III was inactivated in the absence of ascorbate and markedly inhibited by cyanide, 5,5′-dithiobis-(2-nitrobenzoic acid) and p-chloromercuribenzoate. The molecular weight of P III was estimated to be 28 000 by both gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Both P II and P III strongly reacted with a monoclonal antibody raised against spinach leaf ascorbate peroxidase whereas P I did not react with it. P III is left to be defined ascorbate peroxidase but these observations suggest that it can be considered as an ascorbate peroxidase peculiar to roots. The content of ascorbate in roots increased rapidly in the early stages of germination and this was followed by an increase in ascorbate-peroxidizing activity accompanied by increased superoxide dismutase activity. Oxidation of ascorbate by peroxidase activity and the absence of ascorbate oxidase activity suggest that P II and P III function to remove H2O2 at an early stage in roots, whose catalase activity is less than 2% that of the described peroxidase activity." @default.
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- W2031449649 date "1996-05-01" @default.
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- W2031449649 title "Presence of ascorbate-peroxidizing enzymes in roots of Brassica campestris L. cv. Komatsuna" @default.
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- W2031449649 doi "https://doi.org/10.1016/0168-9452(96)04413-5" @default.
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