Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

"Chitin-specific" peroxidases in plants.

I V Maksimov1, E A Cherepanova, R M Khairullin

  • 1Institute of Biochemistry and Genetics, Ufa Scientific Center of the Russian Academy of Sciences, Ufa, 450054, Russia. phyto@anrb.ru

Biochemistry. Biokhimiia
|April 16, 2003
PubMed
Summary

Plant peroxidases show varied chitin-binding abilities, with some isoforms activating in chitin presence. This chitin-binding activity is linked to plant defense mechanisms against fungal pathogens.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Search for biocontrol agents among endophytic lipopeptide-synthesizing bacteria Bacillus spp. to protect wheat plants against Greenbug aphid (Schizaphis graminum).

Vavilovskii zhurnal genetiki i selektsii·2024
Same author

The effect of salicylic and jasmonic acids on the activity of SnAGO genes in the fungus Stagonospora nodorum Berk. in in vitro culture and during infection of wheat plants.

Vavilovskii zhurnal genetiki i selektsii·2024
Same author

[Dynamics of adreneractivity after transfer of myocardial infarction: annual observation].

Terapevticheskii arkhiv·2021
Same author

[Signal molecules involved in the regulation of the wheat defense response to Septoria nodorum infection].

Prikladnaia biokhimiia i mikrobiologiia·2018
Same author

[Inhibition of IAA oxidase activity of wheat anionic peroxidase by chitooligosaccharides].

Prikladnaia biokhimiia i mikrobiologiia·2018
Same author

[RNA-silencing of anionic peroxidase gene decreases the potato plant resistance to Phytophthora infestans (Mont.) de Bary].

Molekuliarnaia biologiia·2015

Area of Science:

  • Plant biochemistry
  • Molecular biology
  • Plant pathology

Background:

  • Plant peroxidases are enzymes involved in various physiological processes.
  • Chitin, a component of fungal cell walls, can act as a signal molecule for plants.
  • The interaction between plant peroxidases and chitin is not fully understood.

Purpose of the Study:

  • To investigate the chitin-binding activity of different plant peroxidase isoforms.
  • To explore the effect of chitin on peroxidase activity.
  • To correlate chitin-peroxidase interactions with plant defense mechanisms.

Main Methods:

  • Extraction and purification of plant peroxidases.
  • Assay of peroxidase activity in the presence of chitin.
  • Chitin-binding assays to fractionate isoperoxidases.

Related Experiment Videos

  • Analysis of anionic and cationic isoperoxidase binding.
  • Main Results:

    • Crude plant extracts showed increased peroxidase activity with chitin.
    • Specific anionic isoperoxidases from oat, rice, horseradish, radish, peanut, and tobacco sorbed onto chitin.
    • Anionic and cationic isoperoxidases from pea, galega, cucumber, and zucchini also sorbed onto chitin.
    • Chitin-induced peroxidase activation was linked to hypersensitive reactions and lignification.

    Conclusions:

    • Plant peroxidases exhibit differential chitin-binding properties based on their isoform type (anionic/cationic).
    • Chitin-binding peroxidases may play a role in inhibiting fungal growth.
    • The structural characteristics of isoperoxidases are important for their chitin-binding and potential anti-fungal functions.