CYTOCHROME-P450 MONOOXYGENASE AND GLUTATHIONE-S-TRANSFERASE ACTIVITY OF 2 AUSTRALIAN TERMITES - MASTOTERMES DARWINIENSIS AND COPTOTERMES ACINACIFORMIS

The major detoxication enzymes have been characterized in preparations of two economically important termite species. Mastotermes darwiniens is microsomes contained a similar quantity of total cytochrome P450 as Coptotermes acinaciformis but the activities of aldrin epoxidase (AE) , 7-ethoxyresorufin O-deethylase (EROD) and 7-ethoxycoumarin O-deethyl ase (ECOD) were 4.5, 5.8 and 17 times higher, respectively. Compared w ith other insects, AE activity in these two termite species is low, ER OD activity moderate and ECOD activities are high, especially in M. da rwiniensis. The cytosolic GST activity of C. acinaciformis toward chlo ro-3,5-dinitrobenzene (CDNB) was 3.13 mu mol min(-1) mg(-1), > 3 fold higher activity than M. darwiniensis cytosol. Apparent K-m values of 1 .87 mM for CDNB and 0.84 mM for glutathione were determined in C. acin aciformis cytosol. 7,8-Benzoflavone dramatically reduced EROD activity in microsomes of both termite species but had significantly lower inh ibitory effect on ECOD activity. The addition of SKF 525A to termite m icrosomes inhibited both EROD and ECOD activities. Multiple isoenzymes of cytochrome P450 in termites are indicated by these findings. The d istinctly different substrate specificities and lambda(max) of the CO difference spectra from M. darwiniensis and C. acinaciformis microsome s may arise from differences in the cytochrome P450 isoenzymes between the two species.