Glutathione transferases and glutathione-binding proteins of termites: purification and characterisation.

Termites have an important role in the cycling of carbon and trace elements in the biosphere through their degradation of wood, grasses and humus. Glutathione transferases (GSTs) are detoxication enzymes found in all organisms; GSTs are known to protect insects from the toxic effects of plant chemicals and pesticides. The activities and characteristics of termite GSTs were investigated in three Australian termite families. Multiple GST isozymes were purified from whole body preparations of the three termite species by affinity chromatography and subsequent chromatofocusing. Termite GSTs exhibited a broad range of activities toward model substrates but were most active with 1-chloro-2,4-dinitrobenzene. The pI values of termite GSTs ranged between 7.4 and 5.8, while the apparent molecular weights of subunits ranged between 25.9 and 27.7 kDa. The N-terminal sequence of a glutathione-binding protein that was purified from Mastotermes darwiniensis was similar to the N-terminal sequence of a streptococcal protein of unknown function previously implicated in glomerulonephritis in humans.