Cytochrome P450 monooxygenase and glutathione S-transferase activity of two Australian termites: Mastotermes darwiniensis and Coptotermes acinaciformis

V S Haritos; John R J French; J T Ahokas

doi:10.1016/0965-1748(94)90021-3

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Cytochrome P450 monooxygenase and glutathione S-transferase activity of two Australian termites: Mastotermes darwiniensis and Coptotermes acinaciformis

Journal article

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Cytochrome P450 monooxygenase and glutathione S-transferase activity of two Australian termites: Mastotermes darwiniensis and Coptotermes acinaciformis

V S Haritos, John R J French and J T Ahokas

Insect Biochemistry and Molecular Biology, Vol.24(9), pp.929-935

1994

DOI: https://doi.org/10.1016/0965-1748(94)90021-3

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Abstract

Biochemistry and Cell Biology

Zoology

cytochrome

P450

monooxygenases

glutathione

S-transferases

termites

Isoptera

The major detoxication enzymes have een characterized in preparations of two economically important termite species. Mastotermes darwiniensis 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-deethylase (ECOD) were 4.5, 5.8 and 17 times higher, respectively. Compared with other insects, AE activity in these two termite species is low, EROD activity moderate and ECOD activities are high, especially in M. darwiniensis. The cytosolic GST activity of C. acinaciformis toward chloro-3,5-dinitrobenzene (CDNB) was 3.13 μmol min-1mg-1, > 3 fold higher activity than M. darwiniensis cytosol. Apparent Km values of 1.87 mM for CDNB and 0.84 mM for glutathione were determined in C. acinaciformis cytosol. 7,8-Benzoflavone dramatically reduced EROD activity in microsomes of both termite species but had significantly lower inhibitory effect on ECOD activity. The addition of SKF 525A to termite microsomes inhibited both EROD and ECOD activities. Multiple isoenzymes of cytochrome P450 in termites are indicated by these findings. The distinctly different substrate specificities and Î»max of the CO difference spectra from M. darwiniensis and C. acibnaciformis microsomes may arise from differences in the cytochrome P450 isoenzymes between the two species.

Details

Title: Cytochrome P450 monooxygenase and glutathione S-transferase activity of two Australian termites: Mastotermes darwiniensis and Coptotermes acinaciformis
Authors: V S Haritos (Author) - RMIT University
John R J French (Author) - University of the Sunshine Coast - Faculty of Science, Health and Education
J T Ahokas (Author) - CSIRO Division of Forest Products
Publication details: Insect Biochemistry and Molecular Biology, Vol.24(9), pp.929-935
Publisher: Pergamon
Date published: 1994
DOI: 10.1016/0965-1748(94)90021-3
ISSN: 0965-1748
Organisation Unit: University of the Sunshine Coast, Queensland
Language: English
Record Identifier: 99450080802621
Output Type: Journal article

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