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Title: Role of anionic isoforms of peroxidase during phytopathogenic infection of plants from the family Malvaceae

Author
item AKHUNOV, A - Sadykov Institute
item GOLUBENKO, N - Sadykov Institute
item KHASHIMOVA, N - Sadykov Institute
item BERESNEVA, YU - Sadykov Institute
item ABDURASHIDOVA, N - Sadykov Institute
item MUSTAKIMOVA, E - Sadykov Institute
item BOKOV, A - Sadykov Institute
item VSHIVKOV, S - Sadykov Institute
item Stipanovic, Robert - Bob

Submitted to: Chemistry of Natural Compounds
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 3/1/2008
Publication Date: 6/1/2008
Citation: Akhunov, A.A., Golubenko, N.R., Khashimova, N.R., Beresneva, Y.V., Abdurashidova, N.A., Mustakimova, E.C., Bokov, A.F., Vshivkov, S.O., Stipanovic, R.D. 2008. Role of anionic isoforms of peroxidase during phytopathogenic infection of plants from the family Malvaceae. Chemistry of Natural Compounds. 44:352-356.

Interpretive Summary: Plants must continually protect themselves from pathogens. We studied wild and commercial cotton plants and four members more distantly related to cotton which had been infected with a plant pathogen. We found that all of the plants produced enzymes that help protect the plant from the pathogen. The more resistant plants reacted more quickly and produced higher levels of the enzymes after infection compared to the susceptible plants. This work, which shows that these enzymes are important in plant resistance and that the resistant plants recognize the presence of the pathogen more quickly that the susceptible plants, will aid investigators in developing cotton plants that are more resistant to pathogens.

Technical Abstract: An increase of the activity and the appearance of new isoforms (high- and low-molecular-weight) in the isospectrum of peroxidase were noted after the action of the phytopathogen Verticillium dahliae on plants from the family Malvaceae. The temperature was shown to have an effect on the resistance to infection of the studied plants. Isoelectric focusing showed that anionic isoforms of peroxidase had isoelectric points of 4.7 and 3.5.