ESTERASE INHIBITION BY ORGANO-PHOSPHORUS RESIDUES, WITH SOME OBSERVATIONS ON POSSIBLE EFFECTS ON PLANT METABOLISM

Organo-phosphorus residues in tissues of sprayed plants were detected by estimating the esterase-inhibiting activity of their leaf and root extracts. This method was used to examine the anti-esterase effects of mangold plants that had been sprayed with Systox, parathion and Hanane. Extracts of leaves of these treated plants were shown to inhibit added choline esterase for some weeks after treatment. The enzymic hydrolysis of phenyl acetate by extracts of leaves and roots of mangold plants treated with these insecticides was reduced for varying periods of up to 8 weeks.
Assays of parts of bean plants that had been sprayed with demeton-S showed that anti-esterase activity was limited to those parts that had been sprayed: tissues developed subsequent to spraying showed no such effects. Leaves sprayed about z months previously inhibited added choline esterase and showed reduced activity in hydrolysing phenyl acetate. There is some evidence that substances, possibly substrates in the plant enzyme systems affected, accumulate in treated leaves.     

STUDIES IN THE MODE OF ACTION OF INSECTICIDES

Acetylcholine, choline chloride, acetyl-β-methylcholine, benzoylcholine, carbamyl choline, adrenaline and d -tubocurarine are non-toxic when injected into the locust. Prostigmine is also non-toxic, and eserine considerably less toxic to the locust than to man.
The toxic effect of tetraethyl pyrophosphate (TEPP) cannot be antagonized by injection of atropine or enhanced by d -tubocurarine.
The injection of acetylcholine chloride following injection of TEPP does not affect subsequent mortality.
These findings are discussed, and it is suggested that the physiology of the nervous system of the insect is unlike that of the mammal, neither cholinesters nor adrenaline being concerned in it. Phosphorus insecticides are thought to inhibit a general esterase not specifically connected with cholinesters.     

THE INSECTICIDAL ACTIVITY OF PARATHION, ITS ISOMERS AND SOME RELATED COMPOUNDS

Heat treatment of parathion at 140° C. and above resulted in isomerization and then thermal decomposition; the loss of toxicity to Calandra granaria being correlated with a reduction of the thiono-sulphur content. Similar results were obtained with O:O-dimethyl-(4-nitrophenyl)-thiophosphate. Paraoxon, O:S-diethyl-(4-nitrophenyl)-thiophosphate, and O:O-diethyl-S-(4-nitrophenyl)-thiophosphate, although all possessing considerable contact activity, were less insecticidal than parathion; O:O-dimethyl-(4-nitrophenyl)-thiophosphate, on the other hand, was considerably more effective than parathion. O:O- bis (2-chloroethyl)-O-(4-nitrophenyl)-thiophosphate was considerably less toxic than parathion and appeared to have a different mode of action. Compounds, S-ethyl- bis -(4-nitrophenyl)-thiophosphate, O-ethyl- bis -(4-nitrophenyl)-thiophosphate, and triethyl thiophosphate were ineffective as contact insecticides.
In the series of compounds examined, replacement of the group P = S by P = O or alteration in size of the groups attached to the central phosphorus atom caused a reduction of insecticidal activity.     

Isolation and characterization of sialate 9(4)-O-acetylesterase from influenza C virus

An esterase was isolated from influenza C virus with a specific activity from 1.7-5 U/mg protein, and its substrate specificity was tested with various naturally occurring O-acylated sialic acids, synthetic carbohydrate acetates, and other esters. The enzyme hydrolyses only acetic acid esters at significant rates. The non-natural substrates 4-methyl-umbelliferyl acetate, 4-nitrophenyl acetate, and alpha-naphthyl acetate are cleaved at highest hydrolysis rates, followed by the natural substrate N-acetyl-9-O-acetylneuraminic acid. The esterase also acts on N-glycoloyl-9-O-acetylneuraminic acid and, much slower, on N-acetyl-4-O-acetylneuraminic acid; N-acetyl-7-O-acetylneuraminic acid is not hydrolysed. 2-Deoxy-2,3-didehydro-N-acetyl-9-O-acetylneuraminic acid is also a substrate for this enzyme, however, 6-O-acetylated N-acetylmannosamine and glucose are not. Esterification of the carboxyl function of sialic acids strongly reduces or prevents esterase action on O-acetyl groups. The carboxyl ester is not hydrolysed. The relative cleavage rates also depend on the type of the non-sialic acid part of the molecule. N-Acetyl-9-O-acetylneuraminic acid as component of sialyllactose and rat serum glycoprotein shows hydrolysis rates close to the free form of this sugar, while acetyl ester groups of bovine submandibular gland mucin and rat erythrocytes are hydrolysed at slower rates. Gangliosides and 4-O-acetylated glycoproteins are no substrates for the purified enzyme. A slow hydrolysis is observed by incubation of 9-O-acetylated GD1a with intact influenza C viruses. As other natural acetyl esters (acetyl-CoA and acetylthiocholine iodide) are not hydrolysed, the enzyme can be classified as sialate 9(4)-O-acetylesterase (EC 3.1.1.53).     

EMBRYONIC DEVELOPMENT AND ESTERASE ACTIVITY OF EGGS OF PIERIS BRASSICAE IN RELATION TO TEPP POISONING

The embryological development of eggs of Pieris brassicae was studied in relation to the occurrence of enzymes hydrolysing phenyl acetate and acetylcholine. Phenyl acetate is hydrolysed at a high rate at all stages of development of the embryo. Hydrolysis of acetylcholine only becomes appreciable in the later stages of development. The first significant level of hydrolysis of acetylcholine can be correlated with the development of a nervous system in the embryo to a stage where it may be functional.
Aqueous solutions of TEPP were applied to eggs soon after they were laid. Low doses of TEPP allowed a high percentage of eggs to develop to the point of hatching before death occurred. Most fully developed embryos became active before they died. As the dose was increased less development took place and with very high doses little development occurred.
The significance of these results is discussed. The available evidence does not indicate that the poison penetrates slowly nor that it is 'locked up' and later released. The explanation that seems to fit the evidence best is that the poison penetrates rapidly and reacts irreversibly with, probably phosphorylates, one or more components of the egg, the extent of subsequent development depending upon the proportion of a biochemical system or the number of systems inactivated. Whilst inhibition of cholinesterase may play a part in the poisoning process, at least under some conditions, the evidence indicates that the death of the embryo may result from some other cause.     

Characterization and inhibition studies of an α-carbonic anhydrase from the endangered sturgeon species Acipenser gueldenstaedti

An α-carbonic anhydrase (CA, EC 4.2.1.1) was purified and characterized kinetically from erythrocytes of the sturgeon Acipenser gueldenstaedti, an endangered species. The sturgeon enzyme (AgCA) showed kinetic parameters for the CO(2) hydration reaction comparable with those of the human erythrocytes enzyme hCA II, being a highly active enzyme, whereas its esterase activity with 4-nitrophenyl acetate as substrate was lower. Sulphonamide inhibitors (acetazolamide, sulphanilamide) strongly inhibited AgCA, whereas metal ions (Ag(+), Zn(2+), Cu(2+) and Co(2+)) were weak, millimolar inhibitors. Several widely used pesticides (2,4-dichlorophenol, dithiocarbamates, parathion and carbaryl) were also assayed as inhibitors of this enzyme. The dithiocarbamates were low micromolar AgCA inhibitors (IC(50) of 16-18 μM), whereas the other pesticides inhibited the enzyme with IC(50)s in the range of 102-398 μM. The wide use of dithiocarbamate pesticides may be one of the factors enhancing the vulnerability of this sturgeon species to pollutants.     

THE EFFECT OF BODY WEIGHT ON THE RESISTANCE TO INSECTICIDES OF THE LAST-INSTAR LARVA OF DIATARAXIA OLERACEA L., THE TOMATO MOTH

At a constant temperature of 24° C. the final larval instar of Diataraxia oleracea lasts about 10 days, during which its resistance to DDT and γ-BHC as contact insecticides progressively increases up to the 5th or 6th day. It then suddenly decreases, this coinciding with cessation of feeding and the beginning of prepupal formation.
Between the 2nd and the 6th days the gross body weight of the last-instar larva increases from about 0.27 to 0.65g. Under the conditions of the experiments, the LD50 of parathion, as a stomach poison, was linearly related to body weight; on the same basis TEPP was slightly less, and lead arsenate, slightly more, toxic to the larger than to the smaller larvae. However, DDT as a stomach or contact insecticide, and γ-BHC as a stomach poison were notably less toxic to the larger larvae. For example, the increase in LD50 for an increase in larval body weight of × 2 was about × 11 for DDT as a stomach poison and about × 12 as a contact insecticide.
The order of effectiveness of the above insecticides as stomach poisons for the last-instar larva of D. oleracea was parathion > DDT > γ-BHC > TEPP = lead arsenate. Zinc fluoarsenate and rotenone were relatively non-toxic. Larvae of D. oleracea were repelled by food leaf treated with an extract of natural pyrethrins.     

STUDIES OF THE TOXICITY TO WORKER HONEY-BEES (APIS MELLIFERA L.) OF CERTAIN CHEMICALS USED IN PLANT PROTECTION

Laboratory techniques are described for the estimation of the stomach poison, direct and residual film contact poison and fumigant poison effects of chemicals to adult worker honey-bees.
The toxicity of eleven chemicals used in plant protection has been investigated by these methods. The order of effectiveness as stomach and contact poisons was: parathion, TEPP, γ-BHC, dieldrin, aldrin, chlordane, o , o -diethyl- o -ethylmercaptoethyl thiophosphate (constituent of Systox), bisdimethylamino fluorophosphine oxide, toxaphene and the sodium salts of 2:4-D and MCPA: as residual films, dieldrin, aldrin, γ-BHC, parathion, chlordane, and o , o -diethyl- o -ethylmercapto-ethyl thiophosphate (constituent of Systox); toxaphene, TEPP and bisdimethylamino fluorophosphine oxide had no measurable effect; as fumigants, dieldrin, γ-BHC, aldrin, parathion, and chlordane; the remainder had no measurable effect.     

Biochemical characterisation of esterases active in hydrolysing xenobiotics in wheat and competing weeds

Esterase activities toward model xenobiotic substrates ( p -nitrophenyl acetate, naphthyl acetate) and pesticide esters (diclofop methyl, bromoxynil octanoate, binapacryl) have been compared in crude extracts from wheat (Triticum aestivum L.) and Triticum progenitors of wheat. Esterase activities were also determined in the weeds, wild oat ( Avena fatua ) and two populations of black-grass ( Alopecurus myosuroides ), one of which (Rothamsted) is susceptible to herbicides, while the other (Peldon) shows cross-resistance to multiple classes of herbicides. Esterase activity toward the model substrates was highest in wheat, while the weeds were more active in hydrolysing the pesticides. Using isoelectric focussing (pH 4–8), 13 proteins with esterase activity toward α -naphthyl acetate could be resolved in hexaploid wheat (genome AABBDD). The pattern of these activities was most similar to that of the diploid progenitor T. tauschii (DD), excepting a major acidic esterase (pI 4.6), which originated from T. urartu (AA). Resolved esterase activities in the weeds were distinct from those observed in the Tritcum species. However, unlike the case with other classes of xenobiotic-metabolising enzymes, the complement of esterases in the Peldon and Rothamsted populations of black-grass appeared to be identical. In all species, the more basic esterases (>pI 5.0) were sensitive to inhibition by organophosphate and carbamate insecticides, suggesting that they were B-class esterases. In contrast, the acidic wheat esterase (pI 4.6) with the greatest activity toward α -naphthyl acetate was insensitive to insecticides. This wheat-specific esterase was purified 7000-fold by a combination of hydrophobic interaction chromatography, gel filtration and anion-exchange chromatography. The purified esterase behaved as a monomeric 45-kDa protein showing high activity toward p -nitrophenyl acetate and α -naphthyl acetate, but limited activity toward the pesticides.     

Simultaneous azo-coupling method for steroid acetate hydrolyzing enzyme

A simultaneous azo-coupling method for histochemical localization of steroid acetate hydrolyzing enzyme is described. It is based on the observation that d-equilenin, a natural oestrogenic steroid hormone, forms deeply coloured insoluble reaction products with diazonium salts under reaction conditions suitable for histochemical purposes. An acetate at position 3 of d-equilenin is rapidly hydrolysed by tissue esterase and the liberated d-equilenin couples with a diazonium salt to form a coloured precipitate. Steroid acetate hydrolyzing enzyme activity was observed in various tissues of the rat; a comparison with nonspecific esterase activity using alpha-naphthyl acetate as substrate suggested that steroid acetate hydrolyzing enzyme activity represents the activity of one or several isozymes of classical nonspecific esterase. This conclusion has also been drawn previously from biochemical studies using esters of other steroids.     

The insecticides; their hazard in industry and in the home

Chemical, pharmacologic and toxicologic properties of the chlorinated hydrocarbon and organic phosphate insecticides have been reviewed. The chlorinated group present problems if there is either acute or chronic exposure, whereas the problems associated with the organic phosphates develop only in event of acute exposure. Chlorinated hydrocarbon insecticides accumulate in body fat depots and cause both liver and kidney damage while being metabolized and excreted. Organic phosphates destroy cholinesterase and produce effects related to overstimulation of the cholinergic branch of the autonomic nervous system. Barbiturates control the convulsions produced by the chlorinated hydrocarbon insecticides. Atropine blocks most of the effects of the organic phosphate insecticides. These compounds may be grouped in the following order of decreasing toxicity: TEPP, HETP, parathion, OMPA, ENP, aldrin, chlorophenothane, toxaphene, gamma benzene hexachloride, malathon and chlordane.     

THE INSECTICIDES—Their Hazard in Industry and in the Home Part I—Chemistry and Pharmacology

Chemical, pharmacologic and toxicologic properties of the chlorinated hydrocarbon and organic phosphate insecticides have been reviewed. The chlorinated group present problems if there is either acute or chronic exposure, whereas the problems associated with the organic phosphates develop only in event of acute exposure.Chlorinated hydrocarbon insecticides accumulate in body fat depots and cause both liver and kidney damage while being metabolized and excreted. Organic phosphates destroy cholinesterase and produce effects related to overstimulation of the cholinergic branch of the autonomic nervous system. Barbiturates control the convulsions produced by the chlorinated hydrocarbon insecticides. Atropine blocks most of the effects of the organic phosphate insecticides. These compounds may be grouped in the following order of decreasing toxicity: TEPP, HETP, parathion, OMPA, ENP, aldrin, chlorophenothane, toxaphene, gamma benzene hexachloride, malathon and chlordane.     

Isolation and characterization of an intracellular esterase from Lactobacillus casei subsp. casei IFPL731

An intracellular esterase from Lactobacillus casei subsp. casei IFPL731 was purified 1000-fold by ion exchange chromatography and gel filtration chromatography. The relative molecular mass of the native enzyme was 105 kDa, while the subunit molecular mass was estimated to be 38 kDa. The esterase hydrolysed tributyrin and had a preference for esters of short-chain fatty acids (butyrate, caproate and caprylate), while it did not hydrolyse palmitate and sterate esters. The apparent Michaelis-Menten constant of the enzyme on p -nitrophenyl butyrate was 0·3 mmol l⁻¹ while on p -nitrophenyl caprylate, it was 0·04 mmol l⁻¹. The esterase was active over a broad range of pH and temperature values, and retained about 50% of maximal activity at pH 5·0 and 12 °C. Activity was strongly inhibited by 5 mmol l⁻¹ phenylmethylsulphonyl fluoride, β-mercaptoethanol and N -ethylmaleimide, and was stimulated by Zn²⁺ at 1 mmol l⁻¹.     

STUDIES IN THE MODE OF ACTION OF INSECTICIDES

Homogenates of the thoracic nervous system of Locusta migratoria migratoriodes are able to hydrolyse acetylcholine (ACh) and o -nitrophenylacetate (NPA), and this hydrolysis can be inhibited by tetraethylpyrophosphate (TEPP) at approximately the same molar concentration for both substrates. It is possible that one acetyl-esterase is responsible for the breakdown of the two substances, and there is no reason to assume the existence of a specific acetylcholinesterase. In normal horse serum, on the other hand, the pseudocholinesterase is quite distinct from the enzyme responsible for the breakdown of NPA.
In an attempt to correlate the inhibition of the locust nerve cord acetylesterase with toxic activity to insects and mice, four chlorinated diethyl-phenylphosphates were tested as contact poisons against a number of insects and by injection against locusts and mice, and also as in vitro inhibitors of locust nerve cord acetylesterase and horse-serum pseudocholinesterase. The chemicals were the 2-chloro-, 4-chloro, 2:4-dichloro- and 2:4:5-trichloro- analogues of diethyl-phenylphosphate.
Good correlation exists between their in vitro activity against the nerve-cord acetylesterase and their contact activity to aphids, but not between the former and injection toxicity to locusts. No correlation could be established between the inhibition of horse-serum cholinesterase and injection toxicity to mice. It is thought likely that the inhibition of nerve-cord acetylesterase is of greater importance in aphids than in other insects, where the toxic action of the phosphoric esters is at least partly concerned with other vital processes, and that a detoxication mechanism in the mammal breaks down some of the phosphoric esters, but not others.     

N-Butyl-N-methyl-4-nitrophenyl carbamate as a specific active site titrator of bile-salt-dependent lipases

The effect of a series of synthetic carbamates on the human (milk or pancreatic) bile-salt-dependent lipase (cholesterol esterase) was examined. N-isopropyl-O-phenyl, N-methyl-O-phenyl, N-butyl-(4-nitrophenyl), N-phenyl-(4-nitrophenyl), N-butyl-N-methyl and N-pentyl-O-phenyl carbamates were inhibitors of the enzyme activity, while O-isopropyl-N-phenyl, O-methyl-N-phenyl, O-benzyl-N-isopropyl and O-cyclohexyl-N-phenyl carbamates were not even recognized by the enzyme. The N-alkyl chain length is essential for the enzyme inhibition and N-butyl-(4-nitrophenyl) or N-pentyl-O-phenyl carbamates are more potent inhibitors than N-methyl-O-phenyl or N-isopropyl carbamates. The inhibition by reactive carbamates fits the criteria for mechanism-based inhibition: the inhibition is first-order with time, shows saturation kinetics with increasing carbamate concentration and leads to an inactive stoichiometric enzyme-inhibitor complex; the enzyme activity can be protected by a competitive inhibitor. Evidence is shown that the enzymatic nucleophilic attack of carbamates is directed at the carbonyl carbon atom and not the nitrogen atom. The inhibition of bile-salt-dependent lipase does not occur consecutive to the formation of a reactive isocyanate derivative of carbamate but via a tetrahedral intermediate involving essential residues implicated in the enzyme catalytic site. This intermediate evolves by liberation of alcohol (or phenol) and formation of an inactive carbamyl enzyme. Among the carbamates tested, N-butyl-N-methyl-(4-nitrophenyl) carbamate specifically inhibits the bile-salt-dependent lipase; the release of 4-nitrophenol from this carbamate is directly proportional to the enzyme inhibition and it may be defined as a specific active-site titrator for bile-salt-dependent lipases.     

ON THE ASSOCIATION OF NON-SPECIFIC ESTERASE ACTIVITY WITH CENTRAL NERVE MYELIN PREPARATIONS

Abstract— Isolated bovine central nerve myelin sheath preparations showed non-specific esterase activity towards naphthyl ester substrates of increasing chain length from acetate to palmitate. Short chain esters were hydrolysed much faster than long chain substrates by myelin, the specific activity for the hydrolysis of β-naphthyl acetate being the highest. Micro-somal fractions from brain white matter were much higher in esterase activity to all naphthyl ester substrates. NADPH-cytochrome c reductase activity was absent from isolated myelin samples. Distilled water and salt and buffer solutions of different ionic strengths and pH were ineffective in releasing non-specific esterase activity from myelin although tri-potassium citrate caused marked inhibition of the membrane-bound esterase activity. The detergent Triton X-100 released esterase activity from the myelin preparations but at a concentration of 0.1 per cent was also inhibitory.     

An esterase in relation to yolk cell lysis at diapause termination in the silkworm,Bombyx mori

Esterase A is one of the esterase isozymes in eggs of Bombyx mori. The effect of this esterase A on the yolk cells of diapause eggs was examined with a hanging-drop culture in order to discover the mechanism of diapause termination in silkworm eggs.The culture of yolk cells in diapause eggs shows spherical forms with dark fine grains in the central parts, large translucent granules in the outer parts, and a membrane on the exterior. When such yolk cells were incubated with yolk materials of acid-treated or diapause-terminated eggs, they were damaged and cell lysis occurred. This suggested that substance(s) causing the cell lysis were present in diapause-terminated eggs. When esterase A separated electrophoretically from non-diapause eggs and diapause-terminated eggs was added to hanging-drop cultures of yolk cells of diapause eggs, the yolk cells were also greatly affected. That is, a part of the yolk cell membrane was dissolved or disappeared, and the central dark fine grains diffused over the cell causing the whole cell to become dark. A few cells lost almost all of their contents and collapsed. Other esterase fractions and fractions without esterase activity in the electrophoresis exerted little effect on the yolk cells. Furthermore, a parallelism between esterase activity to hydrolyse 2-naphthyl acetate as substrate and the lytic activity on the yolk cell membrane was observed in this esterase A fraction from different sources.From these results it is highly probable that the substance responsible for cell lysis is the esterase A enzyme itself. Diapause termination of silkworm eggs is discussed in relation to the lysis of yolk cells.     

Investigations of the esterase, phosphatase, and sulfatase activities of the cytosolic mammalian carbonic anhydrase isoforms I, II, and XIII with 4-nitrophenyl esters as substrates

The esterase, phosphatase, and sulfatase activities of carbonic anhydrase (CA, EC 4.2.1.1) isozymes, CA I, II, and XIII with 4-nitrophenyl esters as substrates was investigated. These enzymes show esterase activity with 4-nitrophenyl acetate as substrate, with second order rate constants in the range of 753-7706M(-1)s(-1), being less effective as phosphatases (k(cat)/K(M) in the range of 14.89-1374.40M(-1)s(-1)) and totally ineffective sulfatases. The esterase/phosphatase activities were inhibited by sulfonamide CA inhibitors, proving that the zinc-hydroxide mechanism responsible for the CO(2) hydrase activities of CAs is also responsible for their esterase/phosphatase activity. CA XIII was the most effective esterase and phosphatase. CA XIII might catalyze other physiological reactions than CO(2) hydration, based on its relevant phosphatase activity.     

Specificity and induction of undecyl acetate esterase from Pseudomonas cepacia grown on 2-tridecanone

Undecyl acetate esterase from Pseudomonas cepacia grown on 2-tridecanone was strongly inhibited by organophosphates and other esterase inhibitors. Also, p-chloromercuribenzoate at 1 x 10(-4) M showed a 70% inhibition of esterase activity. The enzyme hydrolyzed both aliphatic and aromatic acetate esters at substrate concentrations of 0.25 M. Under these conditions the highest reaction rate was toward undecyl acetate. No lipase or proteolytic activity was demonstrated. Undecyl acetate esterase was classified as a carboxylesterase (B-esterase). Cell-free activity studies on the production of undecyl acetate esterase grown on different carbon sources plus zymogram studies demonstrated that the enzyme was inducible when 2-tridecanone, 2-tridecanol, undecyl acetate and, to a lesser extent, 1-undecanol were growth substrates. Induction of undecyl acetate esterase during oxidation of 2-tridecanone supports the view that undecyl acetate is an intermediate in the degradation of the methyl ketone.     

六种常用杀虫剂对八种蚜虫的选择毒性

作者自1982年开始研究了乐果、氧化乐果、抗蚜威、氰戊菊酯、溴氰菊酯和氯氰菊酯等6种杀虫剂对8种蚜虫的选择毒性.以桃粉大尾蚜Hyalopterus amygdali Blanchard为标准,氧化乐果对桃粉大尾蚜和瓜蚜Aphis gossypii Glover之间的选择毒性指数最高为163.77,乐果和抗蚜威分别是373.24和34.70,而氰戊菊酯仅为1.37.氰戊菊酯最高的选择毒性指数是在桃粉大尾蚜和麦长管蚜Sitobionavenae(F.)之间,也只有6.86,有机磷和氨基甲酸酯杀虫剂对不同蚜虫的选择毒性与乙酰胆碱酯酶(AChE)对巯基试剂(DTNB)的敏感度有明显的相关性,说明其选择毒性与AChE的巯基结合部位有关.同时还发现,抗蚜威对洋槐蚜Aphis robiniae Macchiati和瓜蚜AChE的1₅₀值与其LC₅₀值表现一致.这些都说明了这两类杀虫剂对不同种蚜虫的选择毒性与AChE有关.氰戊菊酯和溴氰菊酯对蚜虫的选择毒性与α-乙酸萘酯羧酸酯酶的活性具有明显的相关性,而与β-乙酸萘酯羧酸酯酶的活性则无任何关系.氯氰菊酯的选择毒性与上述两种酯酶的活性没有任何相关性.