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In type 2 diabetes mellitus (DM2), the impaired functions of the brain insulin system are associated with the weakened insulin transport through the blood-brain barrier due to insulin resistance. Insulin deficiency in the brain can be corrected by intranasal administration of insulin (II), whose effect may be enhanced by intranasal administration of C-peptide (ICP). In this work, we study the effect of treating hyperinsulinemic and normoinsulinemic DM2 rats with ICP (36 µg/rat/day), II (20 µg/rat/day) and ICP+II on metabolic and hormonal parameters. In normoinsulinemic DM2, ICP attenuated thyroid hormone deficiency and enhanced the restorative effects of II on glucose, insulin, and leptin sensitivity. In hyperinsulinemic DM2, ICP was ineffective, and its combination with II weakened the restorative effects of II. Thus, ICP and its combination with II are effective in restoring metabolic and hormonal parameters in normoinsulinemic, but not hyperinsulinemic, DM2.

Abstract A timely and efficient removal of apoptotic cells and their fragments is essential to maintain tissue homeostasis in normal and pathological conditions. Since the removal of apoptotic substrates is executed by the cells endowed with phagocytic activity, the issue of its regulation is of particular interest. In this work, we studied the effect of two biologically active substances, insulin and ganglioside GM1, on phagocytic activity of rat primary astrocytes. We showed that cell incubation with 1 µM insulin significantly decreased the phagocytic activity of astrocytes (58.5% vs. control), whereas the incubation with 10 µM GM1 caused an increase in phagocytic activity (133.4% vs. control). Preincubation of brain astrocytes with GM1 completely blocked the inhibitory effect of insulin. These results can be instrumental in developing novel therapeutic strategies for the treatment of neurodegenerative diseases accompanied by the emergence of apoptotic substrates.

The development of industrial poultry farming requires not only the breeding of new highly productive poultry breeds, but also the development of new rearing technologies and the improvement of standardized nutrition. Currently, in the field of feeding farm animals and poultry an important research area is the search for cheaper non-traditional and affordable feed products that can replace part of the grain in the poultry diet. It is very important to use local raw materials. One of these crops is naked oat, which has the highest energy content, the highest concentration of lysine and methionine among all cereals. The purpose of the researches was to determine the eff ectiveness of using naked oat in compound feed for quails. The results of the influence of complete nutrient-balanced compound feeds with naked oat on zootechnical and economic indicators in the rearing of quails have been presented in the article. It has been found that the live weight of quails in the experimental group has been increased by 3,06 %, while the average daily feed consumption has been increased by 1,83 %. Feed expenditures per 1 kg of live weight gain in the experimental group have been lower by 1,31 % due to the absorption of feed nutrients. According to the results of the balance experiment, the digestibility of raw protein has increased by 1,90, fat by 0,41 %, nitrogen-free extractive substances by 2,77 %. When calculating economic indicators, it has been found that the use of naked oat in compound feed for quails allowed to increase the yield of meat and revenue from its sale by 3,75 %. Despite an increase in the total cost of feed consumed by the experimental group by 2,27 %, the profi t has been received by 9,59 % more. The level of profi tability of quail meat production in the experimental group exceeded the indicator of the control group by 3,40 %.

In order to ensure high productivity of poultry compound feeds are required. However, their production is limited by the lack of high-energy and protein feed in the country. In recent years, many farms are increasingly using the reserve of intensification of feed production, such as the cultivation of new and sparsely distributed forage crops. In this regard, more and more attention is drawn to sugar sorghum, which has received a high rating not only as a productive and drought-resistant crop, but also as the culture that has excellent feed qualities. The results of studying the influence of compound feed with sugar sorghum seeds on zootechnical, physiological and economic indicators when raising broiler chickens have been presented in the article. The researches have been carried out on broiler chickens from the age of one day to 42 days. Two groups of broiler chickens have been formed (control and experimental) per 50 heads in each to conduct the experiment. It has been found during the researches that when input in structure of the diet of 30 % of sugar sorghum the increase of live weight of broilers by 4,16 %, the average daily feed intake 2,82 %, and reduced expenditures of feed per 1 kg of daily gain by 1,67 %. The use of experimental compound feed has increased the digestibility of nutrients by broiler chickens: raw protein by 0,48 %, raw fat by 2,50 %, and raw fiber by 4,93 %. It has been found on the base of the results of anatomical cutting of broiler chicken carcasses that the experimental group contained more edible parts and muscles compared to the control group. The level of profitability of broiler meat production in the experimental group has exceeded the indicator of the control group by 5,4 %.

In recent years, the Russian poultry industry has been successfully developing because of the use of modern crosses, as well as technologies for poultry housing and feeding. The development of quail farming as an eff ective source of dietary and delicacy products is promising. One of the most important conditions for successful breeding of quails is the organization of complete feeding, which involves the use of high-quality protein and energy feed in the diets. It is very important to maximize the use of local raw materials. In this series, a special place is occupied by hulless barley, which is characterized by a reduced content of hard-to-digest fi ber, and therefore has the increased nutritional value for poultry. Therefore, it is of particular relevance to study the input of various varieties of hulless barley in the composition of compound feed for poultry. The purpose of the research was to study the infl uence of compound feed using hulless barley of Siberian selection on the meat productivity of quails. The results of the study on quails using compound feed with 10 % hulless barley have been presented in the article. It has been found that the expenditures of feed per 1 kg of live weight gain in the experimental group of quails have been higher by 3,6 % due to better assimilation of feed nutrients. The live weight of quails in the experimental group has been increased by 4,31 %, while the average daily feed intake has been increased by 0,62 %. Data from the balance experiment have shown that protein digestibility has increased by 1,81 % in the experimental group. It has been found that the use of compound feed with 10 % of hulless barley is of practical signifi cance in relation with the increase in the productivity of quails and the profi tability of meat production by 8,3 %.

Coaching is considered as an innovative personnel-technology aimed at improving and increasing the efficiency of managerial competencies at all levels of interaction. The author developed the stages of implementation of coaching in the company using the GROW model; determined the eff ectiveness of coaching using various forms of implementation; identifi ed the conditions for the development of coaching in the Russian practice and its limiting factors.

Two cholinesterases were identified in the cotton bollworm Helicoverpa (Heliothis) armigera Hbn., that is, acetylcholinesterase from the nervous chain and butyrylcholinesterase from homogenates of larvae. A comprehensive study of the substrate-inhibitor specificity of cholinesterases (based on the modern concept of inhibition by high substrate concentrations), as well as the investigation of anti-enzyme action of 57 irreversible organophosphorus inhibitors, indicated a peculiarity of the enzymological characteristics of the bollworm cholinesterases compared to cholinesterases of arthropods and some mammals.

A study of substrate–inhibitor specificity of mitochondrial monoamine oxidase (MAO) in the hepatopancreas of the adult Kamchatka crab Paralithodes camtschaticus revealed specific catalytic properties of the enzyme. On the one hand, crab hepatopancreas MAO, like its classical hepatic counterpart, can deaminate tyramine, tryptamine, dopamine, serotonin, noradrenalin, benzylamine, β-phenylethylamine and N-methylhistamine but shows no sensitivity to 10 mM semicarbazide. On the other hand, MAO deaminates histamine but not putrescine, two classical diamine oxidase (DAO) substrates. It was established that MAO activity was several times higher toward benzylamine, β-phenylethylamine and N-methylhistamine than toward serotonin and noradrenalin. MAO was also found to be almost 500 times more sensitive to its selective inhibitor deprenyl than to chlorogilyn. A substrate–inhibitory analysis with the use of deprenyl and chloroginyl provides an indirect evidence for the existence of a sole MAO molecular form in the Kamchatka crab hepatopancreas.

This review summarizes the literature data as well as experimental results obtained at our Institute over a period of 50 years on the substrate specificity of cholinesterases–acetylcholine acetylhydrolases (EC 3.1.1.7) and acylcholine acylhydrolases (EC 3.1.1.8). The parameters of enzymatic hydrolysis of oxo- and thiocholine and β-methylcholine esters in different organs and tissues were analyzed in 66 animal species including 22 chordate, 20 insect, 1 mite, 17 mollusk, 4 nematode, and 2 flatworm species. Our substrate specificity studies and extensive data on the inhibitory specificity obtained using irreversible organophosphorous inhibitors and reversible effectors unequivocally indicate that the cholinesterase family is characterized by a clear-cut species and tissue specificity.

We report a pioneering analysis of the interaction between mammalian cholinesterases and 36 acylates and thioacylates of ammonium alcohols with different structure of an alkyl chain between ammonium and etheric atoms and with different structure of a cyclic ammonium group. Among these ethers, which were both substrates and reversible inhibitors of erythrocyte cholinesterase and serum butyrylcholinesterase, specific effectors of both enzymes were identified.

A comparative analysis of enzymological characteristics of cholinesterase (ChE) and monoamine oxydase (MAO) from the optic ganglia was performed in the Pacific squid Todarodes pacificus and Commander squid Berryteuthis magister caught in their four habitats across the Pacific Northwest. A substrate–inhibitor analysis revealed a homogeneity of T. pacificus and B. magister ChE preparations as well as homogeneity of T. pacificus vs. heterogeneity of B. magister MAO preparations. In case of thiocholine derivatives, the rate of hydrolysis induced by T. pacificus ChE was practically independent of the structure of the acyl group, whereas in case of B. magister ChE it was found to decrease in this substrate series. It is only T. pacificus MAO that was found to be able to deaminate also a diaminooxydase substrate histamine. ChE activity was higher in T. pacificus than in B. magister for the whole substrate series, while for MAO the same activity pattern was observed for tyramine, tryptamine and serotonin. In both squids, the sensitivity of ChE to organophosphorus inhibitors containing the dimethylbutyl group was by several orders of magnitude higher than that in mammals. The sensitivity of ChE to the siloxane reversible inhibitors was lower in T. pacificus ChE and much lower in B. magister than in mammals.

To study the influence of onium atom nature on anticholinesterase efficiency of elementorganic derivatives of tetramethylenbisonium compounds as reversible inhibitors of cholinesterase (ChE) - acetyl-ChE from human erythrocytes, butyryl-ChE from horse serum, ChE from the brain of frog Rana temporaria and ChEs from visual ganglia of Pacific squid Todarodes pacificus and individuals of Comman- der squid Berryteuthis magister from different habitats in the northwestern Pacific Ocean were investigated. Bisphosphonium inhibitors were significantly more potent effectors than bisammonium ones, but this may be associated with a significantly increased size and hydrophobicity of onium groups of the former. Bisammonium organosilicon compound and its monoammonium analogue were equally active reversible ChE inhibitors in mammals. First studied bis(phenyliodonium) derivative, which is characterized by a significant increase in the degree of hydrophobicity due to introduction of fluorine atoms in the interonium tetramethylene chain, also had marked anticholinesterase effects on mammalian ChE.

Inorganic tetramethylene bis-onium compounds were studied as reversible inhibitors of various cholinesterases (ChE), i.e., human erythrocyte acetyl-ChE, horse blood serum butyryl-ChE, grass frog Rana temporaria brain ChE, and Pacific squid Todarodes pacificus and commander squid Berryteuthis magister visual ganglia ChE from various habitats in the northwest Pacific Ocean, in order to study the influence of the nature of the onium atom on their anti-ChE activities. bis-Phosphonium inhibitors turned out to be significantly more potent effectors than bis-ammonium compounds, which may actually have been due to the significant increases of size and hydrophobicity of the onium groups. The bis-ammonium organosilicon compound and its monoammonium analog turned out to be equally active as reversible ChE inhibitors in mammals. The bis-phenyliodonium derivative was studied for the first 7time, was characterized by significantly increased hydrophobicity due to introduction of F atoms into the tetramethylene spacer in the onium chain, and exhibited marked anti-ChE activity with respect to mammalian ChE.

To study the effect of the onium atom nature on anticholinesterase efficiency, we tested elementorganic derivatives of tetramethylenbisonium compounds as reversible inhibitors of the following cholinesterases (ChE): acetyl-ChE from human erythrocytes, butyryl-ChE from horse serum, ChE from the brain of the grass frog Rana temporaria, ChEs from visual ganglia of the Pacific squid Todarodes pacificus, and ChE from visual ganglia of the commander squid Berryteuthis magister from different habitats in the Northwestern Pacific Ocean. Bisphosphonium inhibitors were found to be much stronger effectors than bisammonum compounds, although this may be due to a significantly increased size and hydrophobicity of their onium groups. Bisammonium organosilicon compound and its monoammonium analog were equally active as reversible ChE inhibitors in mammals. The first studied bis(phenyliodonium) derivative, which is characterized by a significantly increased hydrophobicity due to the introduction of fluorine atoms to the interonium tetramethylene chain, also exhibited a pronounced anticholinesterase effect on mammalian ChE.

A comparative enzymological investigation of inhibitory specificity of the liver monoamine oxidases (MAO) from the two frog species, lake frog Rana ridibunda and grass frog Rana temporaria, revealed certain interspecies similarities and distinctions of this enzyme. The anti-monoamine oxidase effect of five derivatives of acridine, three derivatives of phenothiazine and one derivative of xanthene (pyronine G) was comparatively analyzed. The tested six-membered tricyclic compounds were shown to exert an irreversible inhibitory effect on the enzyme from both biological sources, displaying the same substrate deamination specificity. Thus, the rate of interaction of acridine and phenothiazine derivatives with the MAO active center in both frog species was considerably higher when activity was determined using noradrenaline versus N-methylhistamine, while that of pyronine G—when activity was determined using N-methylhistamine versus noradrenaline. Interspecies quantitative differences were found in the inhibitory efficacy and degree of selectivity of the tested tricyclic compounds, indicative of the differences in catalytic properties of liver MAO at the interspecies level in the representatives of the genus Rana, family Ranidae. The data of substratespecific inhibitory analysis provide indirect evidence of the existence of two molecular MAO forms in the liver of the studied frog species.

The review presents data on comparative reactivity of 68 cholinesterase preparation from various organs and tissues in a number of vertebrates and invertebrates based on sensitivity to two highly specific and most studied organophosphorus inhibitors--diisopropyl fluorophosphates (DFP) and (2-ethoxymethyl phosphoryl thioethyl) ethyl (methyl) sulphonium sulphomethylat (GD-42). Analysis of these data suggests a great diversity in enzymologic characteristics of cholinesterase preparation in representatives of vertebrates and invertebrates, this variety observed even for closely related enzymes in animals of almost the same level of development.

The substrate and inhibitory specificity of mitochondrial monoamine oxidase (MAO) in the liver of males of the summer form of the chum salmon Oncorhynchus keta was studied. As to the spectrum of deaminated substrates, the hepatic MAO of the chum salmon is similar to MAO of most terrestrial mammals, for eight classical MAO substrates similarity in their substrate characteristics were found. Analysis of the antimonoamine oxidase activity of two derivaties of 2-propinilamine, five derivatives of acridine as well as of pyronine G revealed significant qualitative and quantitative differences as compared to the hepatic enzyme of tuna and whitefish. The compounds tested manifested themselves as irreversible inhibitors of chum salmon's hepatic MAO possessing various efficacy, but lacking the selectivity of action as dependent on the deaminated substrate. The obtained data on the substrate and inhibitory analysis provide an indirect evidence for the presence of a single molecular form of MAO in the chum salmon liver.

A comparative analysis of the effect of the five acridine, three phenothiazine and one xanten (pyronine G) derivatives on the activity of liver mitochondrial monoamine oxidase (MAO) in sexually mature male river lampreys Lampetra fluviatilis has been conducted. Tyramine, dopamine, serotonin, noradrenaline, benzylamine, β-phenylethylamine and N-methylhistamine have been used as substrates for analyzing the monoamine oxidase activity of heterocyclic compounds. The analyzed synthetic hexamerous tricyclic compounds exhibit irreversible inhibition of the enzyme but no specificity depending on the desaminated substrate. The number and identity of heteroatoms in the analyzed heterocyclic compounds have been established to influence their inhibitory efficiency. The data of substrate-inhibitory analysis obtained with the use of the specific substrates provide indirect evidence for the existence of a single MAO form in the lamprey liver.

Specifically synthesized group of benzimid­azole derivatives possessing varying degrees of delocalization of the positive charge in the cation group of the molecule has been studied in order to search for potential cholinergically active compounds and to study the role of the Coulomb interaction in cholinesterase catalysis. These compounds were reversible inhibitors of cholinesterase (ChE) of human erythrocytes, horse serum, brain of the frog Rana temporaria­ and visual ganglia of the Pacific squid Todarodes pacificus in the presence of acetylthio­choline iodide and propionylthiocholine iodide as substrates. The differences in the nature of reversib­le inhibitory effect were observed. The effect of the inhibitor structure and substrate nature, specific for each of the studied inhibitors, on the character of the process of reversible inhibition was found.

The study was performed to check whether the horse blood serum butyrylcholinesterase expresses transferase activity in the presence of several low-molecular aliphatic alcohols, using chromogenic substrate 1-methyl-8-acetoxychinolium iodide whose phenolic hydrolysis product absorbs intensively at 445 nm, whereas the initial ester practically does not absorb within this spectrum area. This allowed measuring simultaneously accumulation of both products of enzymatic hydrolysis: of acetic acid by the potentiometric, while of phenol—by the colorimetric method. Rates of formation of both products of enzymatic hydrolysis are practically equal in experiments with all studied alcohols. This indicates that horse blood serum butyrylcholinesterase under these experimental conditions does not catalyze the transfer of acetyl residue to the studied aliphatic alcohols, i.e. does not have transferase activity.

There was studied action of aliphatic alcohols (ethanol, propanol, isopropanol, n-butanol, isobutanol, sec-butanol, tert-butanol), and pH on various kinds of serum cholinesterase. At inhibition of the cholinesterase hydrolytic activity under effect of alcohols the key role was played not by the total number of carbon atoms in the alcohol molecule, but by the “efficient length” of the carbohydrate chain. The fact that the presence of alcohols did not affect parameters of reversible inhibition of cholinesterase by onium ions tetramethylammonium and choline allows suggesting the absence of action of solvents on specific sorption of acetylcholine in the enzyme active center. With aid of two sets of hydrophobic organophosphorus inhibitors (OPI) (12 compounds), we have managed to estimate both the degree and the character itself of serum cholinesterase.

Research on cholinesterases and effects of their inhibition in the USSR and Russia since 1930-1940s till present is exposed in historical aspects. The first physiological and toxicological effects of cholinesterase inhibition were reported by Alexander Ginetsinsky during World War II, when academic institutions were evacuated from Leningrad to Kazan. The main scientific schools that initiated research on chemistry, enzymology and physiology of cholinesterases and their inhibitors were leaded by Alexandr and Boris Arbuzovs, Victor Rozengart, Viktor Yakovlev, Michael Michelson, Martin Kabachnik, Mikhail Voronkov, Ivan Knunyants, Alexandr Bretskin and others. They investigated the main physiological effects of cholinesterase inhibitors, and analyzed the catalytic mechanisms of cholinesterases and related enzymes. Their contributions are landmarks in the history of cholinesterase research. At the present time revival of research on cholinesterases in different universities and institutes is vivid, in particular at the Moscow State University, research institutes of Russian Academy of Sciences and Kazan Scientific Center.

The review presents data on comparative reactivity of 68 cholinesterase preparation from various organs and tissues in a number of vertebrates and invertebrates based on sensitivity to two highly specific and most studied organophosphorus inhibitors--diisopropyl fluorophosphates (DFP) and (2-ethoxymethyl phosphoryl thioethyl) ethyl (methyl) sulphonium sulphomethylat (GD-42). Analysis of these data suggests a great diversity in enzymologic characteristics of cholinesterase preparation in representatives of vertebrates and invertebrates, this variety observed even for closely related enzymes in animals of almost the same level of development.

The substrate and inhibitory specificity of mitochondrial monoamine oxidase (MAO) in the liver of males of the summer form of the chum salmon Oncorhynchus keta was studied. As to the spectrum of deaminated substrates, the hepatic MAO of the chum salmon is similar to MAO of most terrestrial mammals, for eight classical MAO substrates similarity in their substrate characteristics were found. Analysis of the antimonoamine oxidase activity of two derivaties of 2-propinilamine, five derivatives of acridine as well as of pyronine G revealed significant qualitative and quantitative differences as compared to the hepatic enzyme of tuna and whitefish. The compounds tested manifested themselves as irreversible inhibitors of chum salmon's hepatic MAO possessing various efficacy, but lacking the selectivity of action as dependent on the deaminated substrate. The obtained data on the substrate and inhibitory analysis provide an indirect evidence for the presence of a single molecular form of MAO in the chum salmon liver.

Arylsulfoesters and carbonic lupinin esters are studied for the first time as reversible inhibitors of mammalian blood cholinesterases. Studied in detail is sensitivity of cholinesterases to mono- and bilupinin inhibitors in Commander squid individuals from different habitation zones.

We compared and analyzed data on the sensitivity of four preparations of acetylcholinesterases from humans, rabbit, and housefly heads to the action of a specially synthesized group of quinolizidine organophosphorus inhibitors, whose molecules contained both isomeric unbranched and branched alkoxy derivatives of the phosphoryl group and epimeric lupinine and epilupinine derivatives of the cleaved group. The differences in the characteristics of these compounds helped us to find specific inhibitors of the different acetylcholinesterases and the show the difference in the reactivities of acetylcholinesterases from different animals.

The quaternary phosphonium compounds were found to be reversible inhibitors of cholinesterases of different animals and showed species-specificity of action depending on their inhibitor structure. We have revealed difference in the inhibitory specificity of various acetylcholinesterase preparations. A difference has been shown in inhibitory parameters of optic ganglia of individuals of the squid Berryteuthis magister from different habitat areas. For the first time in comparing phosphonium and ammonium isologues-tetrabutyl- and tributylhexyl derivatives, it has been shown that they are agents practically similar by the character of the anticholinesterase action.

The review presents data on cholinesterase effects of 28 specially synthesized organosilicon compounds (monoonium, organoelement, and bisonium derivatives) studied as reversible inhibitors of acetylcholinesterase (acetyl-ChE) of human erythrocytes, butyryl-ChE of horse blood serum, ChE of brain of common frog Rana temporaria, ChE of the optical ganglia tissue of Pacific squid Todarodes pacificus and of individuals of Commandor squid Berryteuthis magister from various habitats in the Northwestern aquatoria of the Pacific ocean. Among the tested compounds, there are revealed highly specific inhibitors of mammalian ChE as well as of ChE of the B. magister individuals from various habitats.

Kinetic analysis of the activating effect of substrate on the cholinesterase catalysis is performed. There are determined values of coefficient of activation A in the pH zone 5 for the process of hydrolysis of acetylcholine, indophenylacetate (IPhA), and 2,6-dichlorophenolindoph enylacetate (DIPhA) by cholinesterase (ChE) of horse blood serum, as well as of IPhA and DIPhA by ChE of optical ganglia of the Pacific squid Todarodes pacificus. The phenomenon of activation has not been revealed at hydrolysis of phenylacetate by the horse blood serum ChE. The conclusion is made that the cause of the activating effect of substrate on the process of enzymatic hydrolysis by ChEs of different origin is the presence of the onium grouping in the structure of substrates.

In this review a comparative analysis is performed of enzymological characteristics of cholinesterase (ChE) from optic ganglia of individuals of the Commander squid Berryteuthis magister caught in 8 zones of its habitation area in the northern-western Pacific aquatorium, of ChE of the Pacific squid Todarodes pacificus as well as of the “standard” acetylcholinesterase from human erythrocytes and butyrylcholinesterase from horse blood serum. By the method of the substrate-inhibitor analysis there was shown homogeneity of ChE preparations from the B. magister individuals from different habitation zones. Kinetic parameters of the enzymatic hydrolysis of 8 ester substrates are presented as well as the data on study of identity of ChE properties in the B. magister individuals from different habitation zones. Study of the process of the ChE reversible inhibition from the Commander squid individuals under action of 57 mono- and bisonium inhibitors has revealed differences in ChE properties in squid individuals from isolates in different zones of the habitation area, which argues in favor of the existence of intraspecies groups of the Commander squid B. magister.

Summarized are results of the 40-year studies of the Russian biochemists on the comparative-enzymological characteristics of cholinesterase of optic ganglia of the Pacific squid Todarodes pacificus. The review includes comparative evaluation of the cholinesterase activity of various hydrobiont tissues, the proof of enzymatic homogeneity of tissues of the Pacific squid optic ganglia, data on substrate specificity with study of 18 ester substrates as well as detailed study of inhibitory specificity (61 irreversible inhibitors and 49 reversible onium inhibitors). Peculiarity of properties of this enzyme as compared with vertebrate and invertebrate cholinesterases is shown.

The paper deals with a comparative study of various aspects of reactivity (substrate and inhibitor specificity, sensitivity to action of hydrophobic organophosphorus inhibitors, capability for reactivation) of cholinesterase preparations from brain, erythrocytes, and serum of a group of mammals (human, rabbit, rat, cattle, dog, and cat). It has turned out that at preservation of the species and tissue specificity, catalytic properties of the brain and erythrocyte cholinesterases of the same animal species are very close to each other.