Abstract
Malathion resistance in Anopheles stephensi from Pakistan was synergized by triphenyl phosphate, primarily a carboxylesterase inhibitor. There was a slight degree of antagonism with piperonyl butoxide. The major metabolite of malathion in larvae of both the resistant and susceptible strains was malathion monocarboxylic acid. Resistant larvae produced about twice as much of this product as the susceptible larvae. This suggests that a qualitative or a quantitative change in a carboxylesterase enzyme may be the basis of malathion resistance in this strain. Analysis of general esterase levels to α- and β-naphthyl acetate showed that there was no quantitative change in the amount of carboxylesterase enzyme present in the resistant strain as compared to the susceptible.
| Original language | English |
|---|---|
| Pages (from-to) | 149-155 |
| Number of pages | 7 |
| Journal | Pesticide Biochemistry and Physiology |
| Volume | 17 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 1 Apr 1982 |
| Externally published | Yes |