药剂对小菜蛾抗性及敏感品系乙酰胆碱酯酶抑制作用比较

采用浸叶法测定了云南通海、元谋和澜沧的小菜蛾plutella xylostella田间种群对常用杀虫剂的抗药性。结果表明,云南上述地区小菜蛾田间种群对各类杀虫剂均产生了不同程度的抗性。对有机磷类药剂的抗药性为1.74~31.1倍;对菊酯类药剂的抗药性为7.41~764倍;对阿维菌素类药剂则产生了 5.60~4.06×104倍的抗性。通过离体和活体试验测定了药剂对小菜蛾头部乙酰胆碱酯酶(AChE)的抑制作用。敌敌畏和灭多威对通海抗性品系AChE离体和活体内的抑制中浓度(I50)分别是敏感品系的209、26.5倍和2.21、2.16倍;敌敌畏对通海小菜蛾种群的离体和活体内抑制中时间(IT50)小于敏感品系,分别是敏感品系的0.32和0.17倍;而灭多威对通海小菜蛾种群的离体和活体内抑制中时间(IT50)则大于敏感品系,分别是敏感品系的1.37和1.74倍。     

Acetylcholinesterase in selected plant-parasitic nematodes: Inhibition, kinetic and comparative studies

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).     

Effect of some herbicides on CO2 fixation,intermediates pattern,and ruDP-carboxylase and FDPase activities of spinach chloroplasts

We have studied the inhibitory effect of the herbicides phenmediphan, chloroxuron, dinoseb, dichlobenil, dicamba, 2,4-D, 2,4-DB, and 2,4-DP on photosynthetic CO₂ fixation and on the level of intermediates of the CO₂ assimilation cycle by isolated chloroplasts, as well as their in vitro activities on the enzymatic systems ribulose-1,5-diphosphate carboxylase and fructose-1,6-bisphosphatase. Phenmedipham showed the strongest inhibition of CO₂ assimilation, with an I₅₀ of 0.05 μM, followed by chloroxuron and dinoseb, with a 50% inhibition in the range of 0.5–1 μM. A weaker inhibitory effect, with an I₅₀ of 50 μM, is promoted by 2,4-DB, whereas dicamba and 2,4-DP showed this inhibition at 100 μM; dichlobenil and 2,4-D were completely ineffective. In the presence of phenmedipham and chloroxuron, the $\text{trioses-}\text{P}\text{P}\text{-glycerate}$ ratio showed a sharp decrease, which means an inhibition of the P-glycerate reduction step by a low NADPH synthesis; a low ratio is also promoted by 2,4-D, but it may be a consequence of induced collateral metabolic pathways of P-glycerate. Dinoseb showed a 25% inhibition of ribulose-1,5-diphosphate carboxylase activity in the concentration range of 10–100 μM and an I₅₀ of 50 μM of the fructose-1,6-bisphosphatase. Thus these effects could contribute, in addition to the photochemical ones, to an explanation of the dinoseb inhibition of CO₂ assimilation by isolated chloroplasts. The other herbicides tested showed a weak or no effect on these enzyme systems.     

Quantitative structure-activity relationships of the inhibition of photosynthetic electron flow by substituted diphenyl ethers

The effect of 41 substituted diphenyl ethers (derivatives of nitrofen and chloroxuron) on photosynthesis in isolated spinach chloroplasts has been studied. All the chemicals were found to be inhibitors of non-cyclic electron transport; the pI₅₀ values varied from 3.17 to 7.16 (I₅₀ is the molar concentration causing 50% inhibition; pI₅₀= -log I₅₀). Based on their structures, the compounds were divided into four groups; for most groups, a correlation between the inhibition of photosynthesis and physicochemical parameters was found. Lipophilicity proved to be the most important parameter; electronic effects did not play a role. Introduction of substituents into the nitrophenyl ring of nitrofen lowered activity considerably. Nitrofen and and chloroxuron analogues seemed to inhibit at different sites in the electron transport chain. A relationship between inhibition of photosynthesis and herbicidal activity was not clear.     

Selectivity, acetylcholinesterase inhibition kinetics, and quantitative structure-activity relationships of a series of N-(2-oxido-1,3,2-benzodioxa-phosphol-2-yl) amino acid ethyl or diethyl esters

The inhibitory effects of a recently introduced series of the titled compounds on insect and mammalian acetylcholinesterase (AChE) activity were examined, where the median inhibition concentration (I₅₀) and the inhibition kinetic parameters, bimolecular inhibition rate constant (k_i), affinity constant (K_a), and phosphorylation rate constant (k_p), were determined for each compound. Results indicated that all examined dioxaphospholenes had less inhibitory effects on mammalian AChE than fenitrothion, a commercial pesticide with moderate mammalian toxicity. The highest selectivity was obtained with compounds containing glutamic and leucine moieties (2.70 and 2.18, respectively) while selectivity of fenitrothion was 0.93. The low inhibitory effects of the examined dioxaphospholenes on mammalian AChE were attributed to their low phosphorylation rates (k_p < 2.2 min⁻¹) compared to that of fenitrothion (k_p = 4.84 min⁻¹). QSAR equations indicated that the inhibition process is controlled mainly by both the phosphorylation rate (direct effect) and the affinity of compounds toward the enzyme (inverse effect). Although the compounds’ hydrophobicity had no effects on the inhibition process, it affects the compounds’ toxicity since it affects the ability of compounds to penetrate insects to reach the enzyme active site.     

Joint action of natural and synthetic photosystem II inhibitors

The inhibitory action on photosystem II of four sorgoleone analogues, isolated from Sorghum bicolor (L) Moench, and two synthetic inhibitors, diuron and bentazone, was tested by measuring oxygen evolution of thylakoid membranes. The inhibition of oxygen evolution for mixtures of inhibitors was compared with the Additive Dose Model (ADM). ADM assumes that, at a defined response level, the effect of a mixture of inhibitors can be unambiguously expressed by the potency of either of the inhibitors applied separately. The slope of the logistic dose-response curves differed between the inhibitors; sorgoleone analogues had the steepest and bentazone the shallowest slope. The difference in slopes makes the interpretation of the isoboles less general and may reflect the differences in the interaction between the natural and the synthetic inhibitors with the binding site. The results suggest that there may be some limitation to ADM, namely that compounds with the same site of action might have different response curves if their mechanism of binding is different. The joint action of inhibitors follows ADM at I₅₀ . Therefore, the inhibitors can replace each other in any mixture ratio, based on the relative potencies of the pure inhibitors, without changing each other's effect on oxygen evolution. The joint action at I₂₀ and I₈₀ sometimes diverged from ADM. © 1999 Society of Chemical Industry     

Trifluoromethylketones as possible transition state analog inhibitors of juvenile hormone esterase

A series of compounds containing the trifluoromethylketone group have been synthesized utilizing either a modified Grignard procedure or by reacting selected aliphatic bromides or tosylates with the Collman reagent [Na₂Fe(CO)₄]. When tested in vitro as inhibitors of crude juvenile hormone esterase from the hemolymph of the cabbage looper, Trichoplusia ni (Noctuidae), the most active compounds were trifluoromethylketones possessing either a juvenoid-like structure or a straight aliphatic chain. The logarithm of the inhibitory potency of the aliphatic compounds was proportional to their chain length, up to 1,1,1-trifluorotetradecan-2-one (I₅₀ = 1 × 10^?7M). This powerful inhibition was found to be highly selective for JHE, reversible, competitive by Lineweaver-Burk analysis, and was characterized by high affinity of the inhibitor for the esterase (K_i = 3.2 × 10^?9M, K_m JH III = 2 × 10^?7M). Other trifluoromethylketones were shown to be inhibitors of T. ni α-naphthylacetate esterase and bovine trypsin. By analogy with the mechanism of trypsin action, trifluoromethylketones are probably potent inhibitors due to their resemblance to a tetrahedral transition state on the reaction coordinate to the acylated enzyme.     

Differential effects of phenoxy herbicides on light-dependent 14CO2 fixation in isolated cells of C3 and C4 plants

Cells were isolated from the developing leaves of Ipomoea aquatica and Digitaria sanguinalis. The effects of phenoxy alkanoic acid herbicides on light-dependent ¹⁴CO₂ fixation and oxygen evolution in these leaf cells were studied. (2,4-Dichlorophenoxy)acetic acid and (2,4,5-trichlorophenoxy) acetic acid (2,4,5-T and 2,4-D) caused a 20% stimulation of ¹⁴CO₂ fixation at 0.8 × 10^?5M and an inhibition at 1 × 10^?4M in I. aquatica leaf cells. Temperature seemed to have a marked influence on such action. No effect or very little effect was observed in the leaf cells of D. sanguinalis. The nonactive (2,4,6-Trichlorophenoxy)acetic acid (2,4,6-T) caused a similar stimulation of CO₂ fixation as 2,4-D and 2,4,5-T at low concentrations in I. aquatica leaf cells, but no inhibition was observed at high concentration. Increase of hight intensity increased the rate of CO₂ fixation in both control and 2,4,6-T-treated cells; however, the percentage of stimulation remained the same. At stimulatory concentration, all three compounds did not cause any stimulation in either photosystem I and II or photosystem II-mediated oxygen evolution. At higher concentrations, the differential effects of 2,4-D and 2,4,5-T on the light-induced CO₂ fixation and photosystem II-mediated oxygen evolution in the I. aquatica leaf cells and D. sanguinalis mesophyll (ms) cells may be attributed in part to their selective action against dicotyledonous plants.     

Properties of acetolactate synthase from sulfonylurea-resistant Scirpus juncoides Roxb. var. ohwianus T. Koyama

Properties of acetolactate synthase (EC 4.1.3.18; ALS) from sulfonylurea-resistant (SUR) Scirpus juncoides Roxb. var. ohwianus T. Koyama were studied biochemically and physiologically in comparison with those from sulfonylurea-susceptible weed (SUS). GR₅₀ values for growth inhibition and I₅₀ values for ALS inhibition by imazosulfuron were determined for both SUR and SUS. Imazosulfuron controlled the SUS above 80% at the dosage more than 10 g a.i./ha but did not control the SUR at the even great dosage of 1000 g a.i./ha. The rates required for 50% growth inhibition of the SUR relative to the SUS (R/S ratio) were 271-fold. The I₅₀ value for inhibition of ALS from the SUS was 15 nM, compared to I₅₀ of >3000 nM for inhibition of ALS from the SUR. These results suggest that a resistance may due to an altered ALS that is insensitive to imazosulfuron. The K_m (pyruvate) value of ALS from the SUR was similar to the K_m for ALS from the SUS, suggesting that a mutation resulting in resistance does not change the affinity of the enzyme for pyruvate. The specific activity of the SUR ALS was similar to that of the SUS ALS, which indicates that resistance is not an over-expression of the enzyme. ALS activity from both biotypes was inhibited by isoleucine, valine, and leucine in this order. However, the SUR ALS was less sensitive to inhibition by valine than the SUS ALS.     

Inhibition of fatty acid biosynthesis in isolated bean and maize chloroplasts by herbicidal phenoxy-phenoxypropionic acid derivatives and structurally related compounds

The effects of nine phenoxy-phenoxypropionic acid derivatives and structurally related compounds on the incorporation of [¹⁴C]-acetate into free fatty acids in isolated bean and maize chloroplasts were studied. The compounds tested were esters and the corresponding free acids, OH-diclofop, a nonherbicidal metabolite of diclofop in plants, and d and l enantiomers of diclofop. Fatty acid biosynthesis in bean chloroplasts was not affected by all compounds. OH-Diclofop had a weak inhibitory effect on fatty acid synthesis in maize chloroplasts, while free acids were stronger inhibitors than the corresponding esters in the same system. Uptake studies with diclofop-methyl and diclofop indicated that the esters showed higher uptake rates in chloroplasts suspension. d-Diclofop (I₅₀, 9 × 10^?8M) was a more potent inhibitor than l-diclofop (I₅₀, 4 × 10^?6M). This agrees with the low herbicidal activity of the l enantiomer in vivo. The results suggest that the mode of action in this type of herbicide may be closely linked with the inhibition of fatty acid biosynthesis. The tolerance of beans could be based on an insensitivity of the target site.     

Effect of phytoplasmal infection on photosystem II efficiency and thylakoid membrane protein changes in field grown apple (Malus pumila) leaves

We have studied the effect of the apple proliferation phytoplasmal infection on some features of the thylakoids from field grown apple (Malus pumila) leaves. Changes in photosynthetic pigments, soluble proteins, ribulose-1,5-bisphosphate carboxylase, nitrate reductase, photosynthetic activities and thylakoid membrane proteins were investigated. The level of total chlorophyll and carotenoids were reduced in phytoplasma-infected leaves. Similar results were also observed for soluble proteins and ribulose- 1,5-bisphosphate carboxylase activity. The in vivo nitrate reductase activity was significantly reduced in infected leaves. When various photosynthetic activities were followed in isolated thylakoids, phytoplasmal infection caused marked inhibition of whole chain and photosystem II activity while the inhibition of photosystem I activity was only marginal. The artificial exogenous electron donors, diphenyl carbazide and hydroxylamine significantly restored the loss of photosystem II activity in infected leaves. The same results were obtained when F_v/F_m was evaluated by chlorophyll fluorescence measurements. The marked loss of photosystem II activity in infected leaves could be due to the loss of 47, 33, 28–25, 23 and 17 kDa polypeptides. It is concluded that phytoplasmal infection inactivates the donor side of photosystem II. This conclusion was confirmed by immunological studies showing that the content of the 33 kDa protein of the water-splitting complex was diminished significantly in infected leaves.     

In vitro and in vivo analyses of the mechanism of action of SWEP

In vitro experiments with intact chloroplasts from hydroponically grown spinach (Spinacia oleracea L. var. Winter Giant) plants, have shown an I₅₀ value for SWEP (methyl N-3,4-dichlorophenyl) carbamate) of 0.1 μM in PS I and II-linked electron transport H₂0 → NADP⁺. With thylakoid membranes the I₅₀ values for PS II-linked Hill reactions H₂O → [Fe(CN)₆]³⁻ and H₂O → dichlorophenolindophenol are in the range 0.05-0.1 μM, whereas the I₅₀ shifts to 0.45 μM in short PS II-linked transport chain diphenylcarbazide → dichlorophenolindophenol. Trypsination of PS II-enriched particles produces a negligible increase of the I₅₀ value in diphenylcarbazide → dichlorophenolindophenol electron transport, a much smaller increase than occurs with diuron- or atrazine-type inhibitors. All these data show SWEP as a strong inhibitor of electron transport in the Q-B region of the PS II-reducing side. However, it appears to have a different binding site than that of urea and triazine herbicides, either on a trypsin resistant or on a non-surface cluster. As a consequence of the NADPH shortage, SWEP brings about a strong inhibition of CO₂ assimilation, with an I₅₀ of 0.04 μM, and a lower percentage of trioses-P among the intermediates of the Calvin cycle. In vivo experiments have shown a three to five times higher inhibition of PS II-linked electron transport, when SWEP was supplied through the roots than when it was applied to the leaves. We have found I₅₀ values of CO₂ assimilation by isolated chloroplasts of foliar disks of 3 and 5 μM, respectively, when the herbicide was root supplied, as opposed to 10 and 25 μM after leaf application.     

Inhibition of Penicillium duponti carboxylesterase by the fungicides captan and folpet

Captan, folpet, and perchloromethylmercaptan were effective inhibitors of Penicillium duponti p-nitrophenylpropionate esterase activity (I₅₀ = 0.5 – 2 μM) whereas α-naphthyl acetate esterase activity was not affected by the presence of these compounds. Captan and folpet are both equally effective at pH 7.3 and 8.3. The ionic composition of the medium had strong effects on the degree of inhibition produced by all inhibitors but did not alter esterase activity. Neither succinamide nor phthalimide caused inhibition of the p-nitrophenylpropionate esterase activity: The trichloromethylmercaptan portion of these fungicides appears to be responsible for the observed inhibition. The rapidity of captan and folpet inhibition of esterase activity (complete in < 1 min) compared to the rates of spontaneous decomposition ($\text{t}{}_{\mathrm{<mtext>1</mtext><mtext>2</mtext>}}\text{> 1}\text{min}$) and the insensitivity of captan and folpet inhibition to hydrogen ion concentration suggest that generation of spontaneous decomposition products is not required for inhibition. The results are consistent with a mechanism in which the entire fungicide molecule binds to the protein followed by enzyme-promoted reactions of captan and folpet which result in loss of esterase activity.     

Toxicological and biochemical characterizations of AChE in Liposcelis bostrychophila Badonnel (Psocoptera: Liposcelididae)

The toxicological and biochemical characteristics of acetylcholinesterases (AChE) in the resistant and susceptible strains (SS) of Liposcelis bostrychophila were investigated. The two resistant strains were the dichlorvos-resistant strain (DDVP-R) and the phosphine-resistant strain (PH₃-R) with resistance ratios of 22.36 and 4.51, respectively. Compared to their susceptible counterpart, the AChE activity per insect and the specific activity of AChE in DDVP-R and PH₃-R were significantly higher. There were also significant kinetic differences between DDVP-R and PH₃-R. The apparent Michaelis-Menten constant (K_m) for acetylthiocholine iodide (ATChI) was obviously lower in SS than that in PH₃-R, indicating a higher affinity to the substrate ATChI in the susceptible strains. The affinity for the substrate ATChI in DDVP-R and SS were not significantly different. The V_max value of the PH₃-R was significantly greater when compared to the V_max for the SS suggesting a possible over expression of AChE in this resistant strain. The inhibition of AChE to insecticide exposure in vitro revealed that all six insecticides were inhibitory for the extracted AChE’s. Based on the I₅₀ values, AChE of the SS were more sensitive to dichlorvos, paraoxon-ethyl, malaoxon and demeton-S-methyl than those of the two resistant strains. As for carbaryl and eserine, the PH₃-R suggested a significantly higher I₅₀s compared to the susceptible strain, while, no significant differences were found between SS and DDVP-R.     

Structural Effects of N-Arylcarbamoylpyrazolines on Calcium Uptake in Rat Brain Synaptosomes

N-Arylcarbamoylpyrazolines with various substituents at the para position of the carbamoyl benzene ring inhibited ATP-dependent Ca²⁺-uptake in synaptosomes prepared from the rat brain. The activity of these compounds was evaluated as log(1/I₅₀), the reciprocal logarithm of half inhibitory concentration, I₅₀ (m ), from the concentration–response curve for the inhibition of Ca²⁺-uptake. Among the compounds tested, methyl 3-(4-chlorophenyl)-4-methyl-1-[N-(4-trifluoromethylphenyl)carbamoyl]-2-pyrazoline-4-carboxylate was the most potent, the I₅₀ value of which as 9·12×10⁻⁷ m . Variations in the activity in terms of log(1/I₅₀) were quantitatively analysed using a substituent parameter, showing that the higher the electron-withdrawing effect of the substituent, the higher was the activity. The substituent effects were similar to those on insecticidal activity against the Americal cockroach. The higher the inhibitory activity against Ca²⁺ uptake, the higher seemed to be the insecticidal activity. Methyl(4S) - 3 - (4 - chlorophenyl) - 4 - methyl - 1 - [N - (4 - chlorophenyl)carbamoyl] - 2 - pyrazoline -4-carboxylate had higher inhibitory activity against Ca²⁺-uptake and higher in-secticidal activity than the R-isomer, but the difference was greater in theCa²⁺-uptake system.     

Hydrolysis rate and In vitro anticholinesterase activity of fenitrothion and S-methyl fenitrothion

Anticholinesterase activity in vitro of pure fenitrothion, S-methyl fenitrothion (SMF) and mixtures of both was studied using different sources of cholinesterase. SMF was two to three orders as active an inhibitor as fenitrothion. In the mixtures, 1 and 5% SMF significantly influenced the I₅₀ value of fenitrothion. The hydrolysis rates of both compounds are given. A method for the synthesis of pure SMF is also described.     

Inhibition of photosystem II in spinach chloroplasts by trachyloban-19-oic acid

The effect of trachyloban-19-oic acid isolated from Iostephane heterophylla (Asteraceae), was investigated on several photosynthetic activities in spinach thylakoids. The results indicated that this compound inhibited ATP synthesis and uncoupled electron transport, as well as basal and phosphorylating electron flow. Therefore, trachyloban-19-oic acid acts as Hill reaction inhibitor. This compound did not affect photosystem I activity but inhibited uncoupled photosystem II electron flow from H₂O to DCPIP, and has not effect on electron flow from H₂O to SiMo, indicating that the site of inhibition of this compound is at the level of Q_A-Q_B. Chlorophyll a fluorescence measurements confirm the behavior of this diterpene as Q_A-Q_B inhibitor, and in the other hand, this results indicate that a perturbation in the thylakoid membranes at the level of LHC II occurs.     

Inhibition of epoxidation of methyl farnesoate to juvenile hormone III by cockroach corpus allatum homogenates

Radiolabeled methyl farnesoate is epoxidized to juvenile hormone III by an NADPH-dependent reaction occurring in corpus allatum homogenates from the cockroach Blaberus giganteus L. Most of the enzymatically produced juvenile hormone has the 10R configuration described for previously isolated natural juvenile hormones. The unnatural 2Z geometrical isomer of methyl farnesoate is epoxidized by the above system faster than the natural 2E isomer. Several series of chemicals known to be inhibitors of mixed-function oxidases were surveyed as inhibitors of methyl farnesoate epoxidation. The anti-juvenile hormone precocene II caused negligible inhibition at 1 · 10^?4M, whereas the best inhibitor was o-bromophenoxymethyl-imidazole with an apparent I₅₀ of 4 · 10^?7M. None of the inhibitors tested were potent morphogenetic agents on Tenebrio molitor pupae, and they failed to cause precocious development of Oncopeltus fasciatus nymphs. The inhibition of in vitro juvenile hormone biosynthesis suggests the possibility of finding an anti-hormone which acts by blocking juvenile hormone biosynthesis.     

Activation of an O-ethyl S-n-propyl phosphorothiolate,TIA-230, in the central nerve of Spodoptera larvae

TIA-230, O-[1-(4-chlorophenyl)-4-pyrazolyl] O-ethyl S-propyl phosphorothiolate, showed strong insecticidal activity against Spodoptera larvae, in spite of its weak in vitro anti-AChE activity. Head AChE of Spodoptera was, however, inhibited with the progress of TIA-230 intoxication. When the isolated central nerve cord was incubated with TIA-230, AChE in the tissue was strongly inhibited even by concentration (10^?5M) lower than in vitro I₅₀ against AChE (10^?4M). The frequency of spontaneous firing of the nerve cord was increased by treatment of TIA-230 at low concentrations (10^?6–10^?5M) after a latent time of several minutes. The firing was increased by fenitroxon, but without the latent time. The length of the latent time agreed well with the time necessary for rising the inhibition of nerve cord AChE by TIA-230. AChE inhibition of TIA-230 in the nerve cord was reduced by the treatment of piperonyl butoxide, an inhibitor of mixed-function oxidases. From these results, TIA-230 was regarded as being activated oxidatively in the nerve cord to inhibit AChE. Profenofos was also activated in the nerve cord. It was concluded, therefore, that O-ethyl S-n-propyl phosphorothiolate insecticides were activated in the central nerve of the insect.