[TETRAMETHONIUM DERIVATIVES AS REVERSIBLE INHIBITORS OF DIFFERENT CHOLINESTERASES].

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.

[COMPARATIVE SENSITIVITY OF CHOLINESTERASES IN VERTEBRATES AND INVERTEBRATES TO HIGHLY SPECIFIC ORGANOPHOSPHORUS INHIBITORS DIISOPROPYL FLUOROPHOSPHATE (DFP) AND (2-ETHOXYMETHYL PHOSPHORYL THIOETHYL) ETHYL (METHYL) SULPHONIUM SULPHOMETHYLAT (GD-42)].

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.

[Transferase activity of horse blood serum cholinesterase at hydrolysis of 1-methyl-8-acetoxychinolium iodide in the presence of aliphatic alcohols].

To check whether the horse blood serum butyrylcholinesterase expresses transferase activity at the complex ester hydrolysis in the presense of several low-molecular aliphatic alcohols, a study was performed with aid of the chromogenic substrate 1-methyl-8-acetoxychinolium whose phenolic hydrolysis product absorbs intensively at 445 nm, whereas the initial ester in this specter area practically does not absorb. This allowed measuring simultaneously the products of accumulation of both products of enzymatic hydrolysis: of acetic acid by the potentiometric, while of phenol--by the photometric 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 catalize transfer of acetyl residue to the studied aliphatic alcohols, i. e. does not have transefase activity.

[How aliphatic alcohols and ph affect reactional capability of the horse blood serum cholinesterase at its interaction with organophosphorus inhibitors].

There was studied action of aliphatic alcohols (ethanol, propanol, isopropanol, n-butanol, isobutanol, secbutanol, tretbetanol) and pH on various kinds of reactional capability the serum cholinesterase. At the alcohols-affected inhibition of the cholinesterase hydrolytic activity, the determining role was played not the total number carbon atoms in the alcohol molecule, but by the "effective length" of the carbohydrate chain. The fact that the presence of alcohols did not affect parameters of the reverse cholinesterase inhibition with onium ions tetramethylammonium and choline allows suggesting the absence of effect solvents on specific acetylcholine sorption in the enzyme active center. With aid of two rows of hydrophobic organophosphorus inhibitors (OPI), we have managed to estimate both the degree and the character itself of the modifying action of alcohols and pH on the process of irreversible inhibition of serum cholinesterase.

[The high-pressure chemistry, barophysiological chemistry, comparative enzymology of cholinesterase the 100th anniversary from the birth of A. P. Brestkin].

There are exposed the main landmarks of the scientific biography of Professor Aleksandr Pavlovich Brestkin, connected with his investigations in the field of chemistry of high pressures, physiological chemistry of caisson disease, kinetics of esterase catalysis, and in comparative enzymology of cholinesterases.

[Reversible lupininin inhibitors of cholinesterases of mammalian blood and of optical ganglia of individuals of the commander squid Berryteuthis magister from different zones of species areal].

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 bislupinin inhibitors in Commander squid individuals from different habitation zones.

[From metabolism to comparative biochemistry of toxic organophosphorus compounds. To the 100th anniversary from the birth of V. I. Rozengart].

The main stages of the scientific biography of Professor Victor losifovich Rozengart are exposed: his works on muscle bioenergetics, discovery of the pathway of creatinine synthesis, his development of novel concepts of pathways of metabolism of organophosphorus xenobiotics, creation of biochemical grounds of selective toxicity as well as studies in the new field whose one of its founders he is--comparative biochemistry of toxic organophosphorus compounds.

[Derivatives of lupinin and epilupinin as ligands of various cholinesterases].

Literature data have been summarized on interaction of cholinesterases of some mammals and arthropods with a group of isomer derivatives of alkaloid lupini and its epimer epilupinin. As substrates of cholinesterases of several mammals there are studied 8 acetates containing in their molecules the chinolysidin bicycle with different structure of N-alkyl radical, which showed certain elements of specificity of action. For 2 isomer esters that are derivatives of the protonated base of the lupinin and epilupinin structures, differences in their substrate characteristics were revealed. The polyenzyme analysis if anticholinesterase efficiency was performed for 30 organophosphorus inhibitors that are dialkoxyphosphorus derivatives of lupinin and epilupinin; as a result, quite a few peculiarities of their action depending on their structure were revealed. Several tested compounds turned out to act as specific inhibitors of cholinesterases of some mammals and arthropods.

[To the 80-anniversary of cholinesterase. The cholinesterase club in Sechenov Institute of Evolutionary Physiology and Biochemistry].

For the second half of the XX century, Sechenov Institute of Evolutionary Physiology and Biochemistry of the Russian Academy of Sciences was the center of the Russian cholinesterase investigations ("the Russian cholinesterase club"). The close cooperation with chemists-syntheticians of different scientific schools provided success and fruitfulness of this scientific search. All these years, there was preserved dualism of this investigation: a study of the mechanism of functioning and kinetics of cholinesterase catalysis as well as the comparative-enzymological character of studies of cholinesterases of the animals being at different levels of evolutionary development.

[Quaternary phosphonium reversibile inhibitors of cholinesterases of different animals].

Quaternary phosphonium compounds were found to be reversible inhibitors of cholinesterases of various animals and showed species-specificity of action depending on the inhibitor structure. It became possible to reveal difference in inhibitory specificity of various preparations of acetylcholinesterases. A difference has been shown in inhibitory parameters of the series of phosphonium toward cholinesterase of visual ganglia of individuals of the squid Berryteuthis magister from different zones of the habitat areal. For the first time, when comparing phosphonium and ammonium isologues - tetrabutyl- and tributylhe-xyl derivatives, it has been shown that they are agents practically similar by the character of anticholinesterase action.

[Siliconorganic reversible inhibitors of cholinesterases of various animals].

The review present data on cholinesterase effects of 28 specially synthesized siliconorganic compounds (monoonium, clementorganic, 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.

[Comparative-enzymological study of cholinesterases from optic ganglia of the Commander squid Berryteuthis magister individuals inhabiting different zones of the species areal].

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 areal 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 heterogeneity 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 inhibitory specificity with use of 20 irreversible organophosphorus inhibitors, which show 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 of squid individuals from isolates in different zones of the habitation areal, which argues in favor of the existence of intraspecies groups of the Commander squid B. magister.

[Comparative-enzymological study of cholinesterase of the Pacific squid Todarodes pacificus].

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 the comparative evaluation of the cholinesterase activity of various hydrobiont tissues, the proof of enzymatic homogeneity of the tissue 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.

[Comparative-enzymologic study of phosphatase activity of hydrobionts from Pacific Ocean].

Activities of acid phosphatase are studied with use as substrates of phenyl phosphate, alpha- and beta-glycerophosphates in various organs and tissues of a large group of industrial hydrobionts of the Pacific basin (12 fish species, 7 invertebrate species. and one mammalian species) and of alkaline phosphatase in various organs of the Commander (Berryteuthis magister) and the New Zealand (Nototodarus sloani sloani) squids. Intertissue and interspecies differences have been revealed in the substrate and inhibitory specificity of the studied enzyme preparations. The method of isolation and a partial purification of preparations of acid phosphatase from tissue of gonads and of alkaline phosphatase from tissues of kidney and liver of individuals of industrial squid species is described.