“Chitin-Specific” Peroxidases in Plants

I. V. Maksimov^*, E. A. Cherepanova, and R. M. Khairullin

Institute of Biochemistry and Genetics, Ufa Scientific Center of the Russian Academy of Sciences, pr. Oktyabrya 69, Ufa, 450054 Russia; fax: (3472) 35-6100; E-mail: phyto@anrb.ru

^* To whom correspondence should be addressed.

Received December 17, 2001; Revision received February 5, 2002

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The activity of various plant peroxidases and the ability of their individual isoforms to bind chitin was studied. Some increase in peroxidase activity was observed in crude extracts in the presence of chitin. Activated peroxidases of some species fell in the fraction not sorbed on chitin and those of other species can bind chitin. Only anionic isoperoxidases from oat (Avena sativa), rice (Oryza sativa), horseradish (Armoracia rusticana), garden radish (Raphanus sativus var. radicula), peanut (Arachis hypogaea), and tobacco (Nicotiana tabacum Link et Otto) were sorbed on chitin. Both anionic and cationic isoforms from pea (Pisum sativum), galega(Galega orientalis), cucumber (Cucumis sativus), and zucchini (Cucurbita pepo L.) were sorbed on chitin. Peroxidase activation under the influence of chitin was correlated to the processes that occur during hypersensitive reaction and lignification of sites, in which pathogenic fungus penetrates into a plant. The role of chitin-specific isoperoxidases in inhibition of fungal growth and connection of this phenomenon with structural characteristics of isoperoxidases are also discussed.

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KEY WORDS: peroxidase, isoenzymes, chitin, activation, sorption

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