Glutathione S-transferase activity in aquatic macrophytes with emphasis on habitat dependence.

Glutathione S-transferase activity of both the microsomal and soluble fractions was determined in a variety of aquatic macrophytes. The examined enzyme extract was prepared from a combination of leaves and shoots. Four different model substrates were used. The highest conjugation rate was obtained for 1-iodo-2,4-dinitrobenzene, followed by 1-chloro-2,4-dinitrobenzene, p-nitrobenzoyl chloride, and 1,2-dichloro-4-nitrobenzene. Comparison of several samples of Nuphar lutea L. from two different lake areas revealed increased glutathione S-transferase activity in plants from the site contaminated with polyaromatic hydrocarbons.