malathion resistance in musca domestica (diptera: muscidae) in district sargodha, pakistan

7/28/2019 Malathion resistance in Musca domestica (Diptera: Muscidae) in district Sargodha, Pakistan

1/19

Vol 63, No. 7;Jul 2013

447 Jokull Journal

Malathion resistance in Musca domestica(Diptera: Muscidae) in district

Sargodha, Pakistan

Sajida Naseem1, Hafiz Muhammad Tahir1, Shafaat Yar Khan1, Rabia Yaqoob1, Azhar

Abbas Khan2, Muhammad Mohsin Ahsan1, Muhammad Arshad1, Arif Muhammad Khan3

& Zahid Abbas Malik3.

1. Department of Biological Sciences, University of Sargodha, Pakistan.2. Department of Entomology, University College of Agriculture,

University of Sargodha, Pakistan.

3. National Institute for Biotechnology and Genetic Engineering,Faisalabad, Pakistan.

Corresponding author: [email protected]

ABSTRACT

The present study was undertaken to assess the resistance status ofMusca domestica

against malathion in district Sargodha. We also compared the activities of Esterases,

Glutathione S-transferases and Monooxygenases in malathion resistant and susceptible

flies. For the study flies were collected from three different localities i.e., Rehman Pura,

Sultan Colony and Chak No, 75-A, SB. Flies from all studied populations were found

resistant to the tested concentrations of malathion. The activities of esterases among

resistant flies were inhibited in all populations. However, the activities of GST and

Monooxygenases were significantly higher among resistant flies compared to susceptible

flies.We concluded from the study that higher level of GST and Monooxygenases in the

malathion treated flies indicate the involvement of these enzymes in the malathion

resistance. As the high level of melathion resistance is recorded in the flies from all studied

populations, so it is recommended that malathion shouldnt be used any more for control ofhouseflies in the area.

Keywords:Musca domesctica, Esterases, GST and Monooxygenases


2/19

Vol 63, No. 7;Jul 2013

448 Jokull Journal

INTRODUCTION

Houseflies (Diptera: Muscidae) are one of the major public health pests through the

world (Cetin et al., 2006). Although various tactics are being used to manage theirpopulation but the use of insecticides is common one. However, due to repetitive sequential

use of the same insecticides or same mode of action, houseflies has developed resistance to

the insecticides all over the world (Marcon et al., 2003; Shono and Scott, 2003; White et

al., 2007). The mechanisms involved for insecticide resistance in insects may include

increased detoxification or metabolism of the toxicants (Taylor and Feyereisen, 1996; Liu

and Yue, 2000), decreased target site sensitivity (Soderlund, 2005) and decreased rate of

cuticular penetration (Plapp, 1976; Oppenoorth, 1984). Increased metabolic detoxification

is considered one of the important mechanisms for the development of insecticide

resistance in houseflies (Taylor and Feyereisen, 1996; Scott, 1999; Liu and Yue, 2000;

Soderlund, 2005). Detoxification enzyme-based resistance is due to enhanced levels or

modified activities of esetrases, glutathione S- transferases (GST) or monooxygenases

(Patil et al., 1996; Hemingway, 2000).

Esterases are mainly involved in detoxification of carbamates, organophosphates

and to a limited extent in metabolism of pyrethroid (Hemingway and Ranson, 2000). These

enzymes break the ester bond by using water molecule. Esterases cause insecticide

resistance in two ways, either by metabolism of very restricted range of insecticides

containing a common ester bond or by rapid-binding and slow turnover i.e., sequestration

(Herath et al., 1987).

Glutathione S-transferases are multifunctional enzymes which catalyze the

conjugation of reduced glutathione with lipophilic compounds having reactive electrophilic

centers. The resultant products thus formed are more water soluble and easily excretable

from the cell (Booth et al., 1961; Boyland and Chasseand, 1969; Habig et al., 1974). These

enzymes posses a wide range of substrate specificities (Enayati et al., 2005). Glutathione S-

transferases also protect the tissues from the oxidative damage and oxidative stress (Pickett

and Lu, 1989; Enayati et al., 2005). Insects GSTs are involved in metabolism of


3/19

Vol 63, No. 7;Jul 2013

449 Jokull Journal

organophophate, organochlorines and pyrethroid groups (Grant and Matsumura., 1989;

Ranson et al., 1997).

Monooxygenases act by binding with molecular oxygen and receive electrons fromNADPH and results in formation of water (Berge et al., 1998; Li et al., 2007). These

enzymes metabolize insecticides through hydroxylation, epoxidation, dehalogenation,

peroxidation, ester oxidation and nitrogen and thioether oxidation (Wilkinson, 1976; Sono

et al., 1996). Monooxygenases are mainly involved in the metabolism of pyrethroids and to

a lesser extent in the detoxification of organophosphates and carbamates (Feyereisen,

1999).

The present study was undertaken to assess the resistance status ofM. domectica

against malathion, to estimate and compare the activities of insecticide detoxifying

enzymes (i.e., Esterases, Glutathione S-transferases and Monooxygenases) between

malathion treated and control and fed and unfedM. domestica.

MATERIALS AND METHODS

Sampling

Flies were collected from three different localities of district Sargodha, Punjab,

Pakistan (i.e., Sultan Colony, Rehman Pura and Chak No. 75-A, SB) by using sweep net.

Collected flies were released in glass jars (12 cm long and 10 cm wide).

The mouth of each jar was covered with mesh cloth and brought to the laboratory in the

Department of Biological Sciences, University of Sargodha. Only the adult flies of almost

same size were used in the study.

Residual bioassays

Residual bioassays at the recommended field dose (2.28 mg/ml), half field dose

(1.14 mg/ml) and double field dose (4.56 mg/ml) were performed to find out resistant

population ofMusca domestica. For this purpose sixty flies were randomly selected and

divided into control and experimental groups (n=30 in each group, 15 males and 15


4/19

Vol 63, No. 7;Jul 2013

450 Jokull Journal

females). Both groups were fed up to the satiation level on mixture of water, thick paste of

condensed milk and sugar. The experimental group was exposed to malathion impregnated

filter paper for one hour while control group to the filter paper impregnated in distilled

water. After one hour of exposure, flies were transferred to clean jars. The mortality was

recorded after every four hours till 24 hours. Sugar water (10%) was provided to the flies

throughout the experimental period (Kaufman et al., 2010). The residual bioassays were

replicated thrice.

Biochemical estimation of insecticide detoxifying enzymes

For the biochemical estimation of enzymes resistant flies obtained from bioassay

experiment were selected and frozen at -20C for 30 minutes in order to make them

immobilize. Later on their legs, wings and abdomens were removed and the rest of the

body of each fly was homogenized in 600 l of phosphate buffer (100 mM, PH 7.0)

containing 0.01% (w/v) of Triton X-100. This crude homogenate was centrifuged at

13000rpm for five minutes at 4C. The supernatant was collected and used as enzyme

source for biochemical estimation of non-specific esterases ( esterases), Glutathione-S-

transferases (GSTs) and Monooxygenases. Confirmed susceptible population was taken as

control for comparison. Enzymes activities of male and females and fed and unfed flies

were also compared.

Estimation of non-specific esterases

To measure the activity of non-specific esterases method of Asperen (1962) was

followed. Beta naphthyl acetate was used as substrates. The reaction mixture contained 60

l homogenate, 60 l substrate solutions (0.1 M) and 1440 l phosphate buffer (100 mM).

The reference solution of the reaction mixture contained 60 l substrate solution and 1500

l phosphate buffer. These mixtures were incubated for 30 minutes at 37C. When

incubation time was over one ml mixture of 1% Fast Blue B salt and 5% sodium dodecyl

sulphate (SDS) in the ratio 2:5 was added to stop the reaction. After 15 minutes these

solutions were transferred to 4 ml cuvettes and optical density was recorded at the

wavelength of 545 nm by using spectrophotometer (UV-1700). Optical density of reference


5/19

Vol 63, No. 7;Jul 2013

451 Jokull Journal

was subtracted from the optical density of solution containing supernatant. The resulting

optical densities (OD) were compared with standard curves to convert the absorbance to

product concentrations. The enzyme activities were expressed as n-mol of product

formed/min/mg of protein.

Estimation of Glutathione-S-transferases

The activity of Glutathione S-trasferases towards 1-chloro-2,4-dinitrobenezene

(CDNB) was estimated according to the method of Habig et al (1974). The reaction mixture

comprised of 100 l 1.0 mM reduced Glutathione, 50 l 1.0 mM 1-chloro-2, 4-

dinitrobenzene (CDNB) and 2.5 ml phosphate buffer (100 mM, PH 7.0) and 50 l of

supernatant. Reference solution for reaction mixture contained 50 l 1.0mM CDNB, 2.5 ml

phosphate buffer (100 mM, PH 7.0) and 100 l 1.0 mM reduced Glutathione. The

absorbance was measured at 340 nm after five minutes of the reaction. Absorbance values

were converted to units of concentration using a molar extinction coefficient () of 9.6 mM

cm-1 for CDNB-GSH conjugate. The activity was calculated as:

CDNB-GSH conjugate = AB\S (increase in 5 min) x 2.7 x 1000

formed in nM /mg protein /min 9.6 x 5 x protein in mg

Estimation of Monooxygenases

Vulule et al. (1999) was consulted to determine the activity of monooxygenases.

Reaction mixture comprised of 100 l of homogenate, 1 ml of 3,3, 5,5- Tetramethyl

benzidine (TMBZ) solution [TMBZ solution was made by dissolving 0.01 g TMBZ in five

ml ethanol and 15 ml 0.25 M sodium acetate buffer (PH 5.0)], 500 l of 0.625 M potassium

phosphate buffer (PPB) atpH 7.0 and 150 l of 3% hydrogen peroxide. Reference solution

for reaction mixture contained one ml TMBZ, 600 l 0.625 M potassium phosphate buffer

(PPB) at pH 7.0 and 150 l 3% hydrogen peroxide. After 10 minutes readings were

recorded at the wavelength of 620 nm. The quantity of monooxygenases was calculated

using the standard curve of cytochrome c.


6/19

Vol 63, No. 7;Jul 2013

452 Jokull Journal

Statistical analyses

Kolmogorov-Smirnov test was used to analyze the normal distribution of the data.

Parametric tests were applied on normally distributed data. For comparison of activities of

different enzymes in control and insecticide treated groups ofM. domestica, two samples

T-test was applied. T-test was also used to compare the activities of enzymes in fed and

unfed flies. All analyses were performed by using Minitab Software (Version 14.1).

RESULTS

Flies from all three populations showed resistance against all tested concentrations

of malathion (Table 1). There was no mortality among the fed females belonging in any of

the three populations exposed to half field rate (1.14 mg/ml) or field rate (2.28 mg/ml) after

24 hours. At double field rate (4.56 mg/ml) the mortality was 6.6% in the flies collected

from the Sultan Colony and Chak No, 75-A, SB and 13.3% in the flies captured from

Rheman Pura. In the starved females exposed to half field rate and field rate of malathion,

there was 6.6% mortality. At double field rate the mortality was 20 % in Sultan Colony and

Rheman Pura, while 13.3% in Chak No, 75-A, SB. No mortality was observed in control

groups (Table 1).

Fed male flies from all three localities showed no mortality at half field rate of

malathion (Table 2). The mortality was 6.6% and 13.3% at field rate and double field rate

respectively. Among starved males the mortality was 6.6% at half field rate and field rate of

malathion and 20% at double field rate in Sultan Colony and Rheman Pura. The mortality

was 13.3% among flies of Chak No, 75-A, SB at double field rate. Again no mortality was

recorded in control groups (Table 2).

Estimation Insecticide detoxifying enzymes

The activity of esterases was inhibited among three populations (both in males

and females) but significant inhibitory effect was recorded in Rehman Pura population

(Table 3 and 4). Significantly higher activity of GST was observed in malathion treated


7/19

Vol 63, No. 7;Jul 2013

453 Jokull Journal

males and females of Sultan Colony and Chak No, 75-A, SB compared to control groups.

The activity was also higher in treated flies of Rehman Pura population but didnt differ

statistically from control groups. The activity of Monooxygenases was also significantly

higher in treated flies of all populations compared to control flies.

The comparison of activity of esterases, GST and Monooxygenases among fed

and starved malathion treated flies is depicted in the Figures 1-3. Significantly higher

activity of esterases was recorded in fed flied of Rehman Pura population. In the

population of Sultan Colony and Chak No, 75-A, SB the difference in activity of

esterases between fed and unfed flies was statistically non significant (Figure 1). Similarly

significantly higher activity of Glutathione-S-transferases was recorded in fed flies of

Sultan Colony and Chak No, 75-A, SB populations (in both males and females) (Figure 2).

No difference in activity of Monooxygenases was recorded among starved and fed flies

(Figure 3).

DISCUSSION

Results of present study revealed that all three populations were found resistance to

all tested concentrations of malathion. Resistance in houseflies against malathion has also

been reported in different parts of the world, like in Malaysia by Bong and Zairi (2010), in

Philippines by Kano et al. (1977) and in Ankara by Sisli et al. (1983). Tang et al. (1994)

had also reported malathion resistance in houseflies. However, Ahmed and Khalequzzaman

(2001) had found the malathion to be less toxic to houseflies in Bangladesh. Sargodha is an

agriculture area of Pakistan and there is an excessive application of insecticides in the area

which might have caused cross resistance in the flies. Bong and Zairi (2010) reported that

resistance in housefly increased with increase in insecticide usage.

Biochemical and molecular methods help us to detect the possible resistance

mechanism in insects. Our findings regarding estimation of enzymes revealed that the

activity of beta esterase was not increased in Malathion treated groups. In Rehman Pura

population significant decrease in activity of beta esterase was recorded in treated flies

compared to control group. These results were close to findings of Taskin and Kence


8/19

Vol 63, No. 7;Jul 2013

454 Jokull Journal

(2004), who recorded the low activity of non specific esterases in malathion resistant strain

of housefly compared to control group. Campbell et al. (1998) recorded 25-50% less

activity of general esterase activity in organophosphate resistant strains than susceptible

strain. The reason for this lower activity of esterases is explained by mutant ali-esterase

hypothesis.

High activity of GST in malathion treated flies was recorded in the present study.

These results are somewhat similar to those reported by Franciosa and Berge (1995) who

found high activity of GSTs in malathion resistant housefly. These results are also similar

to results reported by Taskin and Kence (2004). High activity of GSTs in OP resistant

housefly strain has also been reported by Motoyama et al. (1980). Increase in activity of

monooxygenases was recorded in malathion treated flies of all three populations. Evidence

for increase in activity of monooxygenases against organophosphates in houseflies has also

been reported in different areas of the world (Kasai and Scott, 2000).

In present study we didnt recorded mark differences in the insecticide tolerance

among fed and starved flies. Although the high activity GSTs was recorded in fed

malathion treated flies compared to starved malathion treated groups of different

populations. The reason for this difference in activity of GSTs couldnt be justified in

present study. In order to get more reliable results further research would be required

including investigating other possible mechanism of resistance. We concluded from our

results that resistance in Sultan Colony and Chak No.75-A SB populations against

malathion may be due to elevated activities of monooxygenases and GSTs. However, in

Rehman Pura population high activity of monooxygenases correlates with malathion

resistance. We also concluded, as high level of resistance is recorded in all populations of

Sargodha so malathion shouldnt be used any more for control of housefly in the area.

REFERENCE

Ahmed, M. F., Khalequzzaman, M., 2001. Malathion Tested for Synergism with

Cypermethrin, Phosalone, Phorate and Fenitrothion on Musca domestica L. J. Biol.

Sci. 1 (11), 1028-1030.


9/19

Vol 63, No. 7;Jul 2013

455 Jokull Journal

Asperen, K. V., 1962. A study of housefly esterases by means of a sensitive colorimetric

method. J. Ins. Physiol. 8, 401-416.

Berge, J., Feyereisen, R., Amichot, M., 1998. Cytochrome P450 monooxygenases andinsecticide resistance in insects. Phil. Trans. R. Soc. Lond. B. 353, 1701-1705.

Bong, L. J., Zairi, J., 2010. Temporal fluctuations of insecticides resistance in Musca

domestica Linn (Diptera: Muscidae) in Malaysia.Trop. Biomed.27, 317325.

Booth, I., Boyland, E., Sins. P., 1961.An enzyme from rat liver catalyzing conjugation with

glutathione. Biochem. J., 79, 516-524.

Boyland, E., Chasseaud, L. E., 1969. The role of glutathione and glutathione S-transferases

in mercapturic acid biosynthesis. Adv. Enzymol. 32, 173.

Cetin, H., Erler, F., Yanikoglu, A., 2006. Larvicidal activity of novaluron, a chitin synthesis

inhibitor, against the housefly,Musca domestica. J. Insect Sci.6, 1-4.

Campbell, P. M., Newcomb, R. D., Russell, R. J., Oakeshott, J. G., 1998. Two Different

Amino Acid Substitutions in the Ali-Esterase, E3, Confer Alternative Types of

Organophosphorus Insecticide Resistance in the Sheep Blowfly, Lucilia cuprina,

Insect Biochem. Mol. Biol. 28, 139150.

Enayati, A. A., Ranson, H., Hemingway, J., 2005. Insect glutathione transferases and

insecticide resistance. Insect Mol. Biol. 14, 3-8.

Feyereisen, R., 1999. Insect P450 enzymes. Annu. Rev. Entomol. 44, 507-533.

Franciosa, H., Berge, H. J. B., 1995. Glutathione S-transferases in housefly (Musca

domestica): location of GST-1 and GST-2 families. Insect Biochem. Mol. Biol. 25

(3), 311-317.

Grant, D. F., Matsumura, F., 1989. Glutathione S-transferase 1 and 2 in susceptible and

insecticide resistant Aedes aegypti. Pestic. Biochem. Physiol. 33, 132-143.


10/19

Vol 63, No. 7;Jul 2013

456 Jokull Journal

Habig, W. H., Pabst, M. J., Jakoby, W. B., 1974. Glutathione S-transferase, the first

enzymatic step in mercapturic acid formation. J. Biol. Chem. 249, 7130-7139.

Hemingway, J., 2000. The molecular basis of two contrasting metabolic mechanism ofinsecticide resistance. Insect Biochem.Mol. Biol., 30, 101-109.

Hemingway, J., Ranson, H., 2000. Insecticide resistance in insect vectors of human disease.

Annu. Rev. Entomol. 45, 371-391.

Kano, R., Cabrera, B. D., Hayashi, A., Shinonaga, S., 1977.Resistant levels of houseflies to

six kinds of synthetic insecticides in the Philippines. Southeast Asian J. Trop. Med.

Public. Health. 8, 515-518.

Kasai, S., Scott, J. G., 2000. Overexpression of cytochrome P450 CYP6D1 is associated

with monooxygenase mediated pyrethroid resistance in house flies from Georgia.

Pestic. Biochem. Physiol. 68, 34-41.

Kaufman, P. E., SMann, R., Butler, J. F., 2010. Insecticidal potency of novel compounds on

multiple insect species ofmedical and veterinary importance.Pes. Manag. Sci., 67,

2635.

Li, X., Schuler, M. A. Berenbanm, R., 2007. Molecular mechanism of metabolic resistance

to synthetic and natural xenobiotics. Annu. Rev. Entmol.52, 231-253.

Liu, N. N., Yue, X., 2000. Insecticide resistance and cross-resistance in the house fly

(Diptera: Muscidae). J. Econ. Entomol. 93, 1269-1275.

Marcon, P., Thomas, G., Siegfried, B., Campbell, J., Skoda, S., 2003. Resistance status of

house flies (Diptera: Muscidae) from southeastern Nebraska beef cattle feedlots to

selected insecticides. J. Econ. Entomol. 96, 1016-1020.

Motoyama, N., Hayaoka, T., Nomura, K., Dauterman, W. C., 1980. Multiple factors for

organophosphorous resistance in the housefly, Musca domestica (L). J. Pesticide

Sci. 5, 393-402.


11/19

Vol 63, No. 7;Jul 2013

457 Jokull Journal

Oppenoorth, F. J., 1984. Biochemistry of insecticide resistance. Pestic. Biochem. Physiol.

22, 187-193.

Patil, N. S., Lole, K. S., Deobagkar, D. N., 1996. Adaptive larval thermotolerance andinduced cross-tolerance to propoxur insecticide in mosquitoes Anopheles stephensi

an intensive chicken farm of Northern Italy. J. Environ. Sci. Health.46,480-485.

Pickett, C. B., Lu, A. Y., 1989. Glutathione S-transferases: gene structure, regulation, and

biological function. Annu. Rev. Biochem. 58, 743-764.

Plapp, F. W., 1976. Biochemical genetics of insecticide resistance. J. Annu. Rev. Entomol.

21, 179-197.

Ranson, H., Prapanthadara, L., Hemingway, J., 1997. Cloning and characterisation of two

glutathione S-transferases from a DDT resistant strain of Anopheles gambiae.

Biochem. J. 324, 97102.

Scott, J. G., 1999. Cytochromes P450 and insecticide resistance. J. Insect Biochem. Mol.

Biol. 29,757-777.

Shono, T., Scott, J. G., 2003. Spinosad resistance in the housefly, Musca domestica, is due

to a recessive factor on autosome 1. Pestic. Biochem. Physiol.75,1-7.

Sisli, M. N., Bosgelmez, A., Kocak, O., Porssuk, H., 1983. [The effects of Malathion,

fenitrothion and propoxur on the housefly, Musca domestica. (diptera: Muscidae),

populations]. Microbiyol Bul. 17, 49-62.

Soderlund, D. M., 2005. Sodium channels. In: Comprehensive Molecular Insect Science.

Gilbert, L. I., Iatrou, K. and Gill, S. S, (eds). Elsevier Pergamon. pp 1-24.

Sono, M., Roach, M. P., Coulter, E. D., Dawson, J. H., 1996. Hemecontaining oxygenases.

Chem. Rev. 96, 28412888.


12/19

Vol 63, No. 7;Jul 2013

458 Jokull Journal

Tang, R., Montada, D., Navarro, A., Garca, F. A., 1994. [Status of insecticide resistance in

4 strains of Musca domestica collected in animal farms]. Rev. Cubana Med. Trop.

46,167-170.

Taskin, V., Kence, M., 2004. The Genetic Basis of Malathion Resistance in Housefly

(Musca domestica L.) Strains From Turkey.Rus., J. Genet. 40, 12151222.

Taylor, M., Feyereisen, R., 1996. Molecular biology and evolution of resistance to

toxicants. Mol. Biol. Evol. 13, 719-734.

Vulule, J. M., Beach, R. F., Atieli, F. K., McAllister, J. C., Brogdon, W. G., Roberts, J. M.,

Mwangi, R. W., Hawley, W. A., 1999. Elevated oxidase and esterase levelsassociated with permethrin tolerance in Anophelesgambiae from Kenyan villages

using permethrin impregnated nets. Med. Vet. Entomol. 13, 239-244.

White, W., McCoy, C., Meyer, J., Winkle, J., Plummer, P., Kemper, C., Starkey, R.,

Snyder, D., 2007. Knockdown and mortality comparisons among spinosad-,

imidacloprid-, and methomyl-containing baits against susceptible Musca domestica

(Diptera: Muscidae) under laboratory conditions. J. Econ. Entomol. 100,155163.

Wilkinson, C. F., 1976. Insecticide biochemistry and physiology. New York. Plenum Press,

p. 768.


13/19

Vol 63, No. 7;Jul 2013

459 Jokull Journal

Table 1: Percent mortality in fed and unfed female flies of different populations exposed

with

different malathion concentrations.

Concentrations

(mg/ml) of

Malathion

%Mortality in fed females after

24 hours of exposure

%Mortality in unfed females

after 24 hours of exposure

Sultan

Colony

Rehman

Pura

Chak

No. 75-

A, SB

Sultan

Colony

Rehman

Pura

Chak

No. 75-

A, SB

0.00 (Control) 0 0 0 0 0 0

1.14 0 0 0 6.6 6.6 6.6

2.28 0 0 0 6.6 6.6 6.6

4.56 6.6 13.3 6.6 20 20 13.3


14/19

Vol 63, No. 7;Jul 2013

460 Jokull Journal

Table 2: Percent mortality in fed and unfed male flies of different populations exposed with

different malathion concentrations.

Concentrations

(mg/ml) of

Malathion

%Mortality in fed males after 24

hours of exposure

%Mortality in unfed males after

24 hours of exposure

Sultan

Colony

Rehman

Pura

Chak

No. 75-A, SB

Sultan

Colony

Rehman

Pura

Chak

No. 75-A, SB

0.00 (Control) 0 0 0 0 0 0

1.14 0 0 0 6.6 6.6 6.6

2.28 6.6 6.6 6.6 6.6 6.6 6.6

4.56 13.3 13.3 13.3 20 20 13.3


15/19

Vol 63, No. 7;Jul 2013

461 Jokull Journal

Table 3: Activity of esterases, Glutathione-S-transferases and Monooxygenases in

control and malathion treated groups of male houseflies.

Test populations

esterases(mM/min/mg of

protein)

(MeanS.E)

Glutathione-S-transferases (nM/mg

of protein/min)

(MeanS.E)

Monooxygenases(g/min/mg of

protein)

(MeanS.E)

Sultan Colony

Control 83.711 348.4 13025

Malathion treated 72.96.0 61.37.4 41361

P-value 0.391 0.028


16/19

Vol 63, No. 7;Jul 2013

462 Jokull Journal

Table 4: Activity of esterases, Glutathione-S-transferases and Monooxygenases in

control and malathion treated groups of female houseflies.

Test populations

esterases(mM/min/mg of

protein)

(MeanS.E)

Glutathione-S-transferases (nM/mg

of protein/min)

(MeanS.E)

Monooxygenases(g/min/mg of

protein)

(MeanS.E)

Sultan Colony

Control 104.515 28.74.3 15947

Malathion treated 92.59.1 58.110 362.640

P-value 0.505 0.034 0.005

Rehman Pura

Control 274.618 12.902.3 92.672

Malathion treated 17319 18.321.6 315.060

P-value 0.003 0.068 0.008

Chak No. 75-A,

SB

Control 84.37.3 10.953.3 19071

Malathion treated 60.49.4 23.83.1 47077

P-value 0.059 0.012 0.018


17/19

Vol 63, No. 7;Jul 2013

463 Jokull Journal

Figure 1. Activity of beta esterase among fed and unfed Malathion treated males (a) andfemales (b).

(a) Males (b) Females


18/19

Vol 63, No. 7;Jul 2013

464 Jokull Journal

Figure 2. Activity of GST among fed and unfed Malathion treated males (a) and females

(b).


19/19

Vol 63, No. 7;Jul 2013

465 Jokull Journal

Figure 3. Activity of monooxygenases among fed and unfed Malathion treated males (a)

and females (b).

(a) Males (b) Females

malathion resistance in musca domestica (diptera: muscidae) in district sargodha, pakistan

Documents