Malathion-resistance in Drosophila Melanogster was studied in susceptible laboratory strains (CS and OR), a heterogeneous intermediate-resistant strain (C1-39), and a more resistant, artificially selected (with malathion). strain (MH19) by comparing the in vitro metabolism of [¹⁴c]-malathion and [¹⁴c]-malaoxon in crude enzyme preparations made from adult flies.
Extracts from all strains were found to contain two enzymatic activities that metabolized malathion and/or malaoxon. One activity degraded malathion to its α- and β-monocarboxylic acids and was designated as malathion-carboxylesterase activity (ME-activity). ME-activity was progressively lost in CS-extracts during reaction with [¹⁴c]-malathion due to inhibition of the enzyme(s) by a tightly bound [¹⁴c]-labeled molecule (not identified) that could not be removed by chromatography on Sephadex G-25. ME-activity, based on initial (0-1 min) rates with or without metyrapone present was similar in all strains and furthermore, the carboxylesterase inhibitors TPP and DEF did not synergize malathion toxicity in either resistant or susceptible strains. It was concluded that carboxylesterase-mediated degradation of malathion was not a factor in the resistance of the C1-39 and MH19 strains. A second enzyme system, microsomal mixed-function oxidases (MFO), converted malathion to malaoxon (activation) and degraded malaoxon to at least two products that were tentatively identified (malaoxon α-and β-monoacids and demethyl-malaoxon). The rate of conversion of malathion to malaoxon was highest in crude extracts of the most resistant MH19 flies, intermediate in C1-39 and could not be detected in the susceptible CS flies while the rate of malaoxon degradation was similar between MH19 and C1-39, but higher than that in the susceptible OR flies. Furthermore, malaoxon (but not malathion) toxicity was most strongly synergized by the MFO-inhibitor MTP in the more resistant strains (MH19 and C1-39) . These results were used along with a previous result that MH19 strain possesses a less sensitive form of the target enzyme, acetylcholinesterase (R.A. Morton, personal communication), to propose a biochemical mechanism that accounts for the increased malathion-resistance of the C1-39 and MH19 strains. / Thesis / Master of Science (MS)
| Identifer | oai:union.ndltd.org:mcmaster.ca/oai:macsphere.mcmaster.ca:11375/23005 |
| Date | 06 1900 |
| Creators | Holwerda, Barry |
| Contributors | Morton, R. A., Biology |
| Source Sets | McMaster University |
| Language | English |
| Detected Language | English |
| Type | Thesis |
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