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1.
The in vitro inhibition potency of some organophosphates (OPs) and carbamates (CAs) which are widely used to control plant-parasitic nematodes on acetylcholinesterase (AChE) of Meloidogyne javanica, Heterodera avenae and Tylenchulus semipenetrans, the major pathogens responsible for the damage of a wide range of crops in Al-Qassim region, Saudi Arabia was examined. AChE of H. avenae activity was 1.58- and 1.51-fold greater than that of T. semipenetrans or M. javanica, respectively. The order of inhibition potency of the tested compounds against T. semipenetrans AChE was: carbofuran > paraoxon > oxamyl > fenamiphos > phorate-sulfoxide > aldicarb, where the corresponding concentrations that inhibited 50% of the nematode AChE activity (I50) were 5 × 10−8, 7 × 10−7, 7.5 × 10−7, 2 × 10−6, 2 × 10−4 and 2 × 10−3 M, respectively. Paraoxon, fenamiphos and carbofuran exhibited high inhibition potency against M. javanica AChE where the I50 values were below 1 nM. Phorate-sulfoxide and aldicarb were potent inhibitors of M. javanica AChE with I50 values of 3.8 and 8 nM, respectively, while oxamyl exhibited low inhibition potency with I50 of 15 nM. Fenamiphos and paraoxon showed the highest I50 values of <100 μM against H. avenae followed by oxamyl (I50 < 1 mM), whereas paraoxon, carbofuran and aldicarb showed low potency with I50 values >1 mM. All the tested compounds exhibited high inhibition potency to AChE of M. javanica than T. semipenetrans or H. avenae. Except phorate-sulfoxide in M. javanica the inhibition pattern and implied mechanism for all the tested compounds for the three nematodes is suggested to be a linear mixed type (a combination of competitive and non-completive type).  相似文献   

2.
A hydrophilic form of acetylcholinesterase (AChE) was purified from N-methyl carbamate susceptible (SA) and highly N-methyl carbamate-resistant (N3D) strains of the green rice leafhopper (GRLH), Nephotettix cincticeps Uhler. Both of purified AChE from SA and N3D strains displayed the highest activities toward acetylthiocholine (ATCh) at pH 8.5. In the SA strain, the optimum concentrations for ATCh, propionylthiocholine (PTCh), and butyrylthiocholine (BTCh) were about 1 × 10−3, 2.5 × 10−3, and 1 × 10−3 M, respectively. However, in the N3D strain, substrate inhibition was not identified for ATCh, PTCh, and BTCh to 1 × 10−2 M. The Km value in the SA strain was 51.1, 39.1, and 41.6 μM and that in the N3D strain was 91.8, 88.1, and 85.2 μM for ATCh, PTCh, and BTCh, respectively. The Km value in the N3D strain indicated about 1.80-, 2.25-, and 2.05-fold lower affinity than that of the SA strain for ATCh, PTCh, and BTCh, respectively. The Vmax value in the SA strain was 70.2, 30.5, and 4.6 U/mg protein and that in the N3D strain was 123.0, 27.0, and 14.5 U/mg protein for ATCh, PTCh, and BTCh, respectively. The Vmax value in the N3D strain was 1.75- and 3.15-fold higher for ATCh and BTCh than that in the N3D strain. However, it was 1.13-fold lower for PTCh. The increased activity of AChE in the N3D strain is due to the qualitatively modified enzyme with a higher catalytic efficiency. The bimolecular rate constant (ki) for propoxur was 27.1 × 104 and 0.51 × 104 M−1 min−1 in the SA and N3D strain and that for monocrotophos was 0.031 × 104 and 2.0 × 104 M−1 min−1 in the SA and N3D strain. AChE from the N3D strain was 53-fold less sensitive than SA strain to inhibition by propoxur. In contrast, AChE from the N3D strain was 65-fold more sensitive to inhibition by monocrotophos than AChE from the SA strain. This indicated negatively correlated cross-insensitivity of AChE to propoxur and monocrotophos.  相似文献   

3.
The activity of the mutant CYPBM3 “21B3”, which is able to use hydrogen peroxide as the final electron acceptor, was evaluated against two major environmental pollutants; organochlorine and organophosphorus pesticides. This evolved CYP from Bacillus megaterium is able to transform a variety of structurally different pesticides. The catalytic parameters for two organochlorine; dichlorophen (kcat = 9.2 min−1, KM = 64.1 μM) and linuron (kcat = 226.5 min−1, KM = 468.2 μM), and two organophosphorus compounds; parathion (kcat = 10.9 min−1, KM = 59.3 μM) and chlorpyrifos (kcat = 9.2 min−1, KM = 226.5 μM) were determined giving catalytic efficiencies between 0.143 and 1.107 min−1 μM−1. CYPBM3 “21B3” has the ability to both activate and detoxify organophosphorus pesticides, as demonstrated by the chemical nature of the reaction products. The capacity to transform structurally diverse compounds together with the great stability, easy production and relatively inexpensive cofactors needed, makes CYPBM3 “21B3” an enzyme with a potential use on the environmental field.  相似文献   

4.
Some inhibition kinetic properties and in vivo inhibition of the plasma juvenile hormone esterase from the cabbage looper (Trichoplusia ni Hübner) by one phosphoramidothioate and two trifluoromethylketones were examined. O-ethyl,S-phenyl phosphoramidothioate was shown to react irreversibly with the enzyme in a time-dependent manner, and the inhibition reaction can be factored into a reversible step with a dissociation constant, Kd, of 4.55 × 10?5M followed by a phosphorylation step with a rate constant, k2, of 1.98 min?1. The phosphorylated enzyme did not show spontaneous recovery after 48 hr of dialysis. On the other hand, the two trifluoromethylketones were shown to act as reversible inhibitors, as their inhibited enzyme was regenerated completely after dialysis. However, 1,1,1,-trifluoro-3-thiooctylpropan-2-one, in contrast to 1,1,1-trifluorotetradecan-2-one, showed progressive time-dependent inhibition, and its reaction with the enzyme followed characteristic bimolecular second-order kinetics with a rate constant, ki, of 3.37 × 107M?1 min?1. The in vivo inhibition data of topically treated larvae at equimolar amounts of the tested compounds indicated rapid penetration, and the stability of the inhibition was higher for the phosphoramidothioate than for the trifluoromethylketones. The relationship of the mechanism of inhibition and the in vivo inhibition of these compounds to the understanding of the interactions between juvenile hormone and juvenile hormone esterase is discussed.  相似文献   

5.
Recovery study was performed at regular intervals to establish the time course of 50% and 100% recovery in neurotransmitter enzyme (acetylcholinesterase, AChE, EC 3.1.1.7) and locomotor behaviour response of mosquito fish, Gambusia affinis exposed to lethal concentration (20.49 mg L−1) of an organophosphorous pesticide, monocrotophos (MCP) for 96 h. In vitro AChE activity studies indicated that MCP could cause 50% inhibition (I50) at 10.2 × 10−5 M. A positive correlation was observed between brain AChE activity and swimming speed during the recovery study. Also, the recovery response of the antioxidant enzymes superoxide dismutase (SOD, EC 1.15.1.1), catalase (CAT, EC 1.11.1.6) and glutathione reductase (GR, EC 1.6.4.2) as well as lipid peroxidation (LPO) as biomarkers of oxidative stress were assessed in viscera of G. affinis. The results showed that the MCP besides its inhibitory effect on target enzyme AChE activity and induction in antioxidant enzyme activities as a characteristic of oxidative stress, which can be used as biomarkers in the pesticide contaminated aquatic streams.  相似文献   

6.
The relationship between the physicochemical properties (molar volume, partition coefficient, and dissociation constant) of slow-acting systemic postemergence xenobiotics and their uptake and translocation to the sites of action was investigated using the nonlinear, dynamic simulation model ERMESSE. When the pKa was held constant at 4.0, the model enables the prediction of the uptake of a systemic xenobiotic as a function of its partition coefficient and molar volume. The model also considered the effects of the physicochemical properties of a systemic xenobiotic on its long-distance translocation within the vascular tissues. For instance, when the log Kow and pKa were held constant at 1.5 and 6.0, respectively, the model predicted a higher translocation rate (55%) for molecules with a small (e.g., MV = 100 cm3 mol−1) as opposed to a large (e.g., MV = 300 cm3 mol−1, 33%) molar volume. In addition, the theoretical predictions from the ERMESSE model showed that any xenobiotic with a molar volume not exceeding 300 cm3 mol−1 could provide an uptake ?50% and a translocation rate ?25% when its log Kow is between −0.5 and 2.5 and its pKa is between 0.0 and 8.0.  相似文献   

7.
The susceptibility to phosalone and biochemical characteristics of acetylcholinesterase (AChE) were compared between susceptible (SS) strain and four field populations of Colorado potato beetle (CPB) collected from commercial potato fields of Hamedan Province in west of Iran. Bioassays involving topical application of phosalone to fourth instars revealed up to 252 fold resistance in field populations compared with the SS strain. Synergism studies showed that although esterase and/or glutathione S-transferase metabolic pathways were present and active against phosalone, they were not selected for and did not have a major role in resistance. It is likely that piperonyl butoxide (PBO) reduced phosalone toxicity by inhibiting bio-activation of phosalone. The affinity (Km) and hydrolyzing efficiency (Vmax) of AChE to selected substrates, namely, acetylthiocholine iodide (ATC), propionylthiocholine iodide (PTC), and butyrylthiocholine iodide (BTC) were examined. AChE inhibition by higher substrate concentration was evident only in the SS strain. In resistant field populations, Aliabad (Aa), Bahar (B) and Dehpiaz (Dp), substrate inhibition at higher concentrations was not seen. There was no definite optimal concentration found for any of the substrates examined. When ATC, PTC, and BTC were used as substrate, the reaction rates of AChE from Yengijeh (Yg) population increased as the concentration of all three substrates were increased, but were almost constant at concentration of ATC ? 3.98, PTC ? 2.8, and BTC ? 5 mM. The susceptible form of AChE had the most efficient ATC hydrolysis but very low BTC hydrolysis activity. In contrast, AChEs from field populations elicited relatively reduced ATC hydrolysis, but relatively increased BTC hydrolysis. The in vitro inhibition potency of some organophosphates (OPs), on AChEs of the field populations and SS strain was determined. The rank order from the most potent inhibitor to the least as determined by their bimolecular reaction constants (Ki) was ethyl paraoxon > diazoxon > methyl paraoxon for AChE from Aa, B, Dp, and Yg populations, respectively, whereas the rank order for the susceptible strain was methyl paraoxon > ethyl paraoxon > diazoxon.  相似文献   

8.
Trehalase, with the target to control insects, nematodes and fungi, is of increasing interest and has been investigated extensively in recent years. Validamycin compounds, as competitive trehalase inhibitors and lead compounds with broad applications have attracted substantial attention as well. In this study, the characterizations of termites trehalase were investigated and the inhibitory effects of validamycin compounds on the termites trehalase were studied as well. Results showed that the termites trehalase is presumably belonging to the acid trehalase with optimal pH of 3.3 and optimal temperature of 37 °C. It was investigated that the concentrations of validoxylamine A (VAA), validoxylamine B (VBB), validamycin A (VA) and validamycin B (VB) required for 50% inhibition IC50 of termites trehalase were calculated to be 14.73 mg l−1, 20.80 mg l−1, 3.17 × 103 mg l−1and 2.24 × 103 mg l−1, respectively. The inhibition kinetic constant Ki values for the above validamycin compounds were 3.2 × 10−6 mol l−1, 1.03 × 10−5 mol l−1, 4.02 × 10−4 mol l−1and 2.69 × 10−4 mol l−1, respectively. Validoxylamine A appeared to be the most potential termites trehalase inhibitor among the four compounds.  相似文献   

9.
In vitro inhibition of electric eel acetylcholinesterase (AChE) by single and simultaneous exposure to organophosphorus insecticides diazinon and chlorpyrifos, and their transformation products, formed due to photoinduced degradation, was investigated. Increasing concentrations of diazinon, chlorpyrifos and their oxidation products, diazoxon and chlorpyrifos-oxon, inhibited AChE in a concentration-dependent manner. IC50 (20 min) values, obtained from the inhibition curves, were (in mol/l): (5.1 ± 0.3) × 10−8, (4.3 ± 0.2) × 10−6 and (3.0 ± 0.1) × 10−8 for diazoxon, chlorpyrifos and chlorpyrifos-oxon, respectively, while maximal diazinon concentration was lower than its IC50 (20 min). Calculated KI values, in mol/l, of 7.9 × 10−7, 9.6 × 10−6 and 4.3 × 10−7 were obtained for diazoxon, chlorpyrifos and chlorpyrifos-oxon, respectively. However, 2-isopropyl-4-methyl-6-pyrimidinol (IMP) and 3,5,6-trichloro-2-pyridinol, diazinon and chlorpyrifos hydrolysis products, did not noticeably affect the enzyme activity at all investigated concentrations. Additive inhibition effect was achieved for lower concentrations of the inhibitors (diazinon/diazoxon ?1 × 10−4/1 × 10−8 mol/l i.e., chlorpyrifos/chlorpyrifos-oxon ?2 × 10−6/3 × 10−8 mol/l), while an antagonistic effect was obtained for all higher concentrations of the organophosphates. Inhibitory power of 1 × 10−4 mol/l diazinon irradiated samples can be attributed mostly to the formation of diazoxon, while the presence of non-inhibiting photodegradation product IMP did not affect diazinon and diazoxon inhibitory efficiencies.  相似文献   

10.
Organophosphothionate insecticide fenitrothion is known as potential toxic pollutant contaminating aquatic ecosystems. The effects of fenitrothion were studied to determine the 96 h LC50 value on Nile tilapia (Oreochromis niloticus) and investigate histopathological responses of fish exposed to sublethal fenitrothion concentrations. Data obtained from the fenitrothion acute toxicity tests were evaluated using the Probit Analysis Statistical Method. The 96 h LC50 value and 95% confidence limit for Nile tilapia (58.70 ± 6.97 g) was estimated as 0.84 (0.68-1.15) mg/L. Behavioral changes were observed closely during the acute toxicity test. The bioassay experiments were repeated three times and static test method was used. Some fish exposed to 96 h 0.1, 0.5 mg/L fenitrothion concentrations showed histopathological alterations in the gills, liver, kidney, brain and testes. Severely deformations were observed at 0.5 mg/L fenitrothion on the gills lamella such as hyperemia, epithelial hyperplasia, fusion and telangiectasis, in the liver tissue such as cloudy swelling, hydropic degenerations and lipid infiltration. In addition hyperemia and hemorrhage observed in kidney tissue and hyperemia was determined in brain tissue.  相似文献   

11.
The oriental tobacco worm, Helicoverpa assulta Guenée, is one of the most destructive pests of tobacco and peppers in China. We determined the susceptibility of H. assulta reared on an artificial diet, chili pepper and tobacco to four insecticides (fenvalerate, phoxim, methomyl, indoxacarb) under laboratory conditions associated with the activities of acetylcholinesterase (AChE), carboxylesterase (CarE) and glutathione S-transferase (GST) in its larvae. H. assulta larvae that were fed with chili pepper were more susceptible to fenvalerate, indoxacarb, and phoxim than those that were fed with tobacco and the artificial diet, but not to methomyl. The larvae that were fed with chili pepper were 3.65-, 2.49-, 1.92- and 2.44-fold more susceptible to fenvalerate, phoxim, methomyl, and indoxacarb than those fed with tobacco, respectively. The AChE activities of H. assulta larvae that were fed with chili pepper and tobacco were 2.12 and 1.07 μmol mg−1 15 min−1, respectively, almost 2-fold difference. The CarE activity of H. assulta larvae that were fed with chili pepper, tobacco and the artificial diet was 4.12, 7.40 and 7.12 μmol mg−1 30 min−1, respectively. Similarly, the GST activities of H. assulta larvae that were fed with chili pepper, tobacco and the artificial diet was 52.02, 79.37 and 80.02 μmol mg−1 min−1, respectively. H. assulta larvae that were fed with chili pepper were more resistance to the tested insecticides. The low activities of AChE and the high activities of CarE and GST lead to H. assulta become more susceptible to the tested insecticides.  相似文献   

12.
Organophosphorus pesticides (OPs) are of environmental significance due to their high toxicity to animals. Binding to plasma proteins may effective influence the toxicological properties of xenobiotics. In an attempt to evaluate the affinity of phenthoate (PTA) to bovine serum albumin (BSA) and inhibitory ability of bound PTA to acetylcholinesterase (AChE), we investigated the interactions between phenthoate (PTA) and bovine serum albumin (BSA) using tryptophan fluorescence quenching and subsequent inhibition on AChE activity by PTA. The results showed that PTA caused the fluorescence quenching of BSA because of the formation of a PTA-BSA complex. Quenching constants (Ksv), determined using the Sterns-Volmer equation to provide a measure of the binding affinity between PTA and BSA at 303, 306, 310 and 313 K were (3.4295 ± 0.0763) × 10−4, (3.2446 ± 0.0635) × 10−4, (3.0434 ± 0.0856) × 10−4 and (2.8262 ± 0.0569) × 10−4 M−1, respectively. The thermodynamic parameters, ΔH and ΔS were −25.04 kJ mol−1 and 168.94 J mol−1 K−1, respectively, which indicated that the electrostatic interactions played a major role in PTA-BSA association. The presence of BSA consistently reduced the inhibitory ability of PTA on AChE, with the relative activity being increased from 46.98 to 61.71% for the concentration range of BSA between 0 and 4.0 g L−1.  相似文献   

13.
In vitro inhibition of house cricket head, house fly head, and bovine erythrocyte acetylcholinesterase by O,O-dimethyl S-aryl phosphorothioates was studied by Main's kinetic treatment. The potency of the compounds as reflected by the bimolecular reaction constants (ki) indicated that house fly head acetylcholinesterase was the most sensitive to the inhibition followed by house cricket head and bovine erythrocyte acetylcholinesterase. There are no linear relationships between the phosphorylation rate constants and the total binding energies for the inhibition of three enzymes by this series of compounds, suggesting that the initial binding and the phosphorylation rate are not related. The structure and activity relationships were analyzed by multiple regression analyses with the use of Hammett's sigma, alkaline hydrolysis rates of the compounds, and pi constants. The hydrophobic bonding of the compound on the enzyme surface as reflected by the pi constant played a significant role in the determination of the potency of the inhibition of house cricket head and house fly head acetylcholinesterase by those compounds. However, the alkaline hydrolysis rates of the compounds, or the Hammett's sigma values seems to play a more important role in the determination of the inhibition of bovine erythrocyte acetylcholinesterase. Moderate insecticidal activity toward house crickets, house flies, and mosquito larvae were found.  相似文献   

14.
Laboratory tests were conducted to compare the effects of various concentrations of lindane and deltamethrin on mature earthworms (Eisenia fetida) cultured in artificial soil during typical acute (14d) and subchronic (42d) exposure periods. The effects of the two pesticides on earthworm mortality, growth inhibition, and cellulase activity were determined for different exposure durations. The toxicity order for earthworm mortality from the 14-day exposure was lindane > deltamethrin, with median lethal concentrations (LC50) of 162.1 and 432.9 mg kg−1, respectively. Earthworms exposed to deltamethrin showed dose-dependent toxic effects on growth and cellulase activity only from the acute exposures, whereas lindane’s effects on these activities were seen correlated with both the acute and subchronic doses. Also, changes in biomass and cellulase activity during the subchronic exposure period appear to be a more sensitive parameter than the LC50 value in assessing pesticidal injury.  相似文献   

15.
In order to gain insight into the development of insecticides with novel modes of action, the effects of salicylidene aniline (a), salicylidene-4-chloroaniline (b), salicylidene-4-bromoaniline (c), and salicylidene-4-nitroaniline (d) on partially purified phenoloxidase (PO) from Pieris rapae L. were investigated. The results showed that the 4 compounds could inhibit PO activity, and the inhibitor concentrations leading to a loss of 50% activity (IC50) were estimated to be 0.025 mmol L−1, 0.732 mmol L−1, 0.471 mmol L−1, and 0.675 mmol L−1, respectively. Meanwhile, all the inhibitors showed reversible competitive inhibition, except (d), which showed reversible mixed inhibition. The KI values were determined as 0.106 mmol L−1, 10.059 mmol L−1, 8.390 mmol L−1, and 20.198 mmol L−1 for the four compounds, respectively. The UV-vis spectra of (a) and (d) in the presence of copper ions and the enzyme showed that (a) could directly chelate the copper ions of PO; however, (d) could neither chelate the additional copper ions nor the copper ions of PO.  相似文献   

16.
Acetylcholinesterase (AChE) was purified from adult heads of the fall armyworm (Spodoptera frugiperda) by using a two-step procedure involving gel filtration on a Sephadex G-200 column and affinity chromatography on a procainamide-ECH Sephadex 4B column. Both susceptible and field strains possessed two AChE isozymes, namely, AChE-1 and AChE-2, with subunit molecular weights of 63.7 and 66.1 kDa. The purified AChE had an apparent Km value of 33.5 μM and a Vmax of 7.07 μmol/min/mg protein in the susceptible strain. The apparent Km and the Vmax were 2.2- and 2.0-fold higher, respectively, in the field strain than in the susceptible strain. The purified AChE from the field strain was 17- to 345-fold less sensitive than that from the susceptible strain to inhibition by carbamates (carbaryl, eserine, methomyl, and bendiocarb) and organophosphates (methyl paraoxon and paraoxon), insensitivity being highest toward carbaryl. The results further support the notion that insensitive AChE played an important role in the insecticide resistance observed in the field strain.  相似文献   

17.
At 37°C and pH 7.4–8.0, five higher O-alkyl analogs of methamidophos and four O-alkyl O-2,5-dichlorophenyl phosphoramidates all were more potent progressive inhibitors of hen brain AChE and neuropathy target esterase (NTE) than was methamidophos itself. For AChE, ka increased from 7.2 × 102 to 1.0 × 105 M−1 min−1 between methyl and n-hexyl S-methyl esters and from 9.3 × 103 to 8.9 × 105 M−1 min−1 between ethyl and n-hexyl dichlorophenyl analogs. For NTE, the ranges were from 16 to 7.9 × 104 for S-methyl esters, and were 9.7 × 104 to 7.8 × 106 M−1 min−1 for dichlorophenyl. S-methyl esters were more active against AChE than against NTE and all the dichlorophenyl esters were more active against NTE than against AChE. Spontaneous reactivation of 75–100% activity without aging of AChE was found after 19 hr incubation at 37°C after inhibition by all nine straight-chain alkyl analogs. After inhibition by O-isopropyl S-methyl phosphorothioamidate, some spontaneous reactivation with complete aging of all remaining inhibited AChE occurred during 19 hr. No spontaneous reactivation or aging of inhibited NTE was detected. It was concluded that the molecular structures of the inhibited enzymes obtained from equivalent compounds in the two series of inhibitors were identical and that the leaving groups were, therefore, S-methyl and O-2,5-dichlorophenyl, respectively. Although hen brain NTE inhibited by methamidophos in vitro did not age, cases of delayed neuropathy in man have been reported and, presumably, require aging as well as inhibition of NTE. Possible explanations of this apparent discrepancy include (i) the fact that methamidophos consists of two chiral forms and that the form seen to be active in vitro may be disposed of preferentially in vivo, (ii) the possibility of activation in vivo to a different inhibitor, (iii) differences between conformation and ease of aging of inhibited NTE in vitro and in vivo, and (iv) species differences.  相似文献   

18.
The fluorescent organophosphate Maretin, O,O-diethyl O-(1–6 naphthaloximido)phosphate, is an optimum analytical reagent for measurement of acetylcholinesterase (AChE) and butyrylcholinesterase cholinesterase (BuChE) normality. It also permits direct measurement of the second-order kinetics of inhibition. Maretin is fluorescent in aqueous solution with excitation at 346 nm and emission at 398 nm. On phosphorylation, the N,N-naphtholoylhydroxylamine leaving group is nonfluorescent. Experimental advantages of this methodology include: readily correctable hydrolysis rate, commercial availability of pure analytical grade Maretin, ease of handling, and no significant side reactions. The bimolecular rate constant (Ki), equilibrium binding constant (Keq), and phosphorylation rate constant (k2) are measured as a function of pH and compared for the two enzymes. Phosphorylation rate data and enzyme activity studies indicate an independent pH functionality between acylation and deacylation for AChE.  相似文献   

19.
Elevated oxidative detoxification is a major mechanism responsible for pyrethroid resistance in Helicoverpa armigera from Asia. Constitutive overexpression of CYP9A12 and CYP9A14 was associated with pyrethroid resistance in the YGF strain of H. armigera. CYP9A12 and CYP9A14 were functionally expressed in the W(R) strain of yeast (Saccharomyces cerevisiae) transformed with a plasmid shuttle vector pYES2. The cell lysates prepared from yeast transformed with CYP9A12 and CYP9A14, respectively, exhibited considerable O-demethylation activities against two model substrates p-nitroanisole (0.59 and 0.42 nmol p-nitrophenol min−1 mg protein−1) and methoxyresorufin (2.98 and 5.41 pmol resorufin min−1 mg protein−1), and clearance activity against the pyrethroid esfenvalerate (8.18 and 4.29 pmol esfenvalerate min−1 mg protein−1). These results provide important evidence on the role of CYP9A12 and CYP9A14 in conferring pyrethroid resistance in H. armigera, and also demonstrate that the yeast expression system can provide necessary redox environment for insect P450s to metabolize xenobiotics.  相似文献   

20.
Valienamine, an aminocyclitol with similar configuration to α-glucose, has a strong inhibitory effect on α-glucosidase. α-Glucosidase plays an important role in insect carbohydrate metabolism. The inhibitory effect of valienamine on the enzymatic activity of honeybee (Apis cerana Fabr.) α-glucosidase was investigated. Our results show that valienamine inhibition of honeybee α-glucosidase was pH- and dose-dependent, but temperature-independent. Valienamine is shown to be a potent and competitive reversible inhibitor of honeybee α-glucosidase in vitro with an IC50 value of 5.22 × 10−5 M and Ki value of 3.54 × 10−4 M at pH 6.5, 45 °C. Valienamine has the potential to be developed into novel insecticides.  相似文献   

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