This research investigated the role of oxidative enzymes in the defense response of buffalograss, Buchloë dactyloides (Nuttall) Engelmann, to Blissus occiduus Barber. Changes in catalase and peroxidase activity were observed in both resistant and susceptible buffalograsses in response to chinch bug feeding. Susceptible plants were shown to have a lower level of catalase activity compared with their respective control plants. By contrast, catalase activities of resistant plants were similar between infested and control buffalograsses throughout the study. Resistant plants had higher levels of peroxidase activity compared with their control plants, whereas peroxidase activities for control and infested susceptible plants remained at similar levels or were slightly lower for infested plants. These findings suggest that chinch bug feeding leads to a loss in catalase activity in susceptible buffalograsses. In contrast, resistant buffalograsses may be able to tolerate chinch bug feeding by increasing their peroxidase activity. Polyphenol oxidase activities were similar between control and infested plants for the buffalograsses evaluated. Among the enzymes examined, no differences in isozyme profiles for peroxidase and polyphenol oxidase were detected between control and infested 378, NE91-118, Cody, and Tatanka plants. Gels stained for catalase identified differences in the isozyme profiles of infested and uninfested 378 plants; however, infested and control NE91-118, Tatanka, and Cody plants has similar isozyme profiles. No differences in protein profiles were observed between chinch bug-infested 378, NE91-118, Cody, and Tatanka plants and their respective uninfested controls.
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1 June 2004
Characterization of Oxidative Enzyme Changes in Buffalograsses Challenged by Blissus occiduus
Tiffany Heng-Moss,
Gautam Sarath,
Frederick Baxendale,
Dana Novak,
Shauna Bose,
Xinhi Ni,
Sharron Quisenberry
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Journal of Economic Entomology
Vol. 97 • No. 3
June 2004
Vol. 97 • No. 3
June 2004
catalase
oxidative enzymes
peroxidase
plant resistance
polyphenol oxidase