Russian Journal of Bioorganic Chemistry

, Volume 36, Issue 3, pp 293–300 | Cite as

Molecular peculiarities of the chitin-binding peroxidases of plants

  • I. V. MaksimovEmail author
  • E. A. Cherepanova
  • O. I. Kuzmina
  • L. G. Yarullina
  • A. A. Akhunov


The chitin-binding ability of isoperoxidases isolated from 23 plants of different species was studied. The activation of peroxidases in a protein extract in the presence of this polysaccharide was found for 14 of the studied plants. Anionic isoperoxidases were shown to be sorbed on chitin and eluted from them with 1M NaCl for 16 of the plant species. Cationic isoforms of the peroxidases of some species of the Fabaceae and Cucurbitaceae plant families also bound to chitin. An immunochemical similarity was found between the chitin-binding isoperoxidases of taxonomically distant plant species (the Pomaceous, Fabaceae, and Cucurbitaceae). Moreover, a high homology of the molecular structures of the polysaccharide-binding sites was revealed for the anionic peroxidases of rice, wheat, oat, zucchini, cucumber, and radish. We propose the existence of a special class of plant peroxidases that bind with polysaccharides (chitin) and participate in the protective reactions of plants against pathogens.

Key words

peroxidase isoenzymes chitin activation sorption 


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Copyright information

© Pleiades Publishing, Ltd. 2010

Authors and Affiliations

  • I. V. Maksimov
    • 1
    Email author
  • E. A. Cherepanova
    • 1
  • O. I. Kuzmina
    • 1
  • L. G. Yarullina
    • 1
  • A. A. Akhunov
    • 2
  1. 1.Institute of Biochemistry and Genetics, Ufa Scientific CenterRussian Academy of SciencesUfaRussia
  2. 2.Sadykov Institute of Bioorganic ChemistryAcademy of Sciences of the Republic Of UzbekistanTashkentUzbekistan

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