Search Results - "Perchenok, A Yu"

Substrate Specificity of Cholinesterases in Various Representatives of the Animal Kingdom by Basova, N. E., Kormilitsyn, B. N., Perchenok, A. Yu, Rozengart, E. V., Saakov, V. S., Suvorov, A. A.

“…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…”
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New Acylate and Thioacylate Effectors of Mammalian Cholinesterases Based on Cyclic Ammonium Alcohols Containing Elements of the Anabasine Structure by Basova, N. E., Kormilitsyn, B. N., Perchenok, A. Yu, Rozengart, E. V., Saakov, V. S., Suvorov, A. A.

“…We report a pioneering analysis of the interaction between mammalian cholinesterases and 36 acylates and thioacylates of ammonium alcohols with different…”
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Tetramethonium derivatives as reversible inhibitors of various cholinesterases by Basova, N. E., Kormilitsyn, B. N., Perchenok, A. Yu, Rozengart, E. V., Saakov, V. S., Suvorov, A. A.

“…To study the effect of the onium atom nature on anticholinesterase efficiency, we tested elementorganic derivatives of tetramethylenbisonium compounds as…”
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Comparative sensitivity of cholinesterases in vertebrates and invertebrates to highly specific organophosphorus inhibitors, diisopropyl fluorophosphate (DFP) and (2-ethoxymethyl phosphoryl thioethyl) ethyl (methyl) sulphonium sulphomethylate (GD-42) by Basova, N. E., Kormilitsyn, B. N., Perchenok, A. Yu, Rozengart, E. V., Saakov, V. S., Suvorov, A. A.

“…The review presents the data on a comparative reactivity of 68 cholinesterase preparations from various organs and tissues in a number of vertebrates and…”
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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) by Basova, N E, Kormilitsyn, B N, Perchenok, A Yu, Rozengart, E V, Saakov, V S, Suvorov, A A

“…The review presents data on comparative reactivity of 68 cholinesterase preparation from various organs and tissues in a number of vertebrates and…”
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Transferase activity of horse blood serum cholinesterase at hydrolysis of 1-methyl-8-acetoxychinolium iodide in the presence of aliphatic alcohols by Basova, N E, Kormilitsyn, B N, Perchenok, A Yu, Rozengart, E V, Saakov, V S, Suvorov, A A

“…To check whether the horse blood serum butyrylcholinesterase expresses transferase activity at the complex ester hydrolysis in the presense of several…”
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Transferase activity of horse blood serum cholinesterase at hydrolysis of 1-methyl-8-acetoxychinolinium iodide in the presence of aliphatic alcohols by Basova, N. E., Kormilitsyn, B. N., Perchenok, A. Yu, Rozengart, E. V., Saakov, V. S., Suvorov, A. A.

“…The study was performed to check whether the horse blood serum butyrylcholinesterase expresses transferase activity in the presence of several low-molecular…”
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How aliphatic alcohols and pH affect reactivity of horse blood serum cholinesterase at its interaction with organophosphorus inhibitors by Basova, N. E., Kormilitsyn, B. N., Perchenok, A. Yu, Rozengart, E. V., Saakov, V. S., Suvorov, A. A.

“…There was studied action of aliphatic alcohols (ethanol, propanol, isopropanol, n -butanol, isobutanol, sec -butanol, tert -butanol), and pH on various kinds…”
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Ligands of cholinesterases of ephedrine and pseudoephedrine structure by Basova, N. E., Kormilitsyn, B. N., Perchenok, A. Yu, Rozengart, E. V., Saakov, V. S., Suvorov, A. A.

“…The paper is a review of literature data on interaction of erythrocytic acetylcholinesterase and of mammalian blood serum butyrylcholinesterase with a group of…”
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Reversible lupinin inhibitors of cholinesterases of mammalian blood and of optical ganglia of individuals of the Commander squid Berryteuthis magister from different zones of species areal by Basova, N. E., Kormilitsyn, B. N., Perchenok, A. Yu, Rozengart, E. V., Saakov, V. S., Suvorov, A. A.

“…Arylsulfoesters and carbonic lupinin esters are studied for the first time as reversible inhibitors of mammalian blood cholinesterases. Studied in detail is…”
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Comparative analysis of sensitivity of cholinesterases to reversible inhibitors by methods of multidimensional statistics by Moralev, S. N, Perchenok, A. Yu

“…Using the methods of factor and cluster analysis, the statistical treatment is performed of data on interaction of seven cholinesterases (ChE)--human…”
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Multivariate statistical analysis of sensitivity of cholinesterases to reversible inhibitors by Perchenok, A Y, Moralev, S N

“…(ProQuest: Abstract omitted; see image)[PUBLICATION ABSTRACT]…”
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TETRAMETHONIUM DERIVATIVES AS REVERSIBLE INHIBITORS OF DIFFERENT CHOLINESTERASES by Basova, N E, Kormilitsyn, B N, Perchenok, A Yu, Rozengart, E V, Saakov, V S, Suvorov, A A

“…To study the influence of onium atom nature on anticholinesterase efficiency of elementorganic derivatives of tetramethylenbisonium compounds as reversible…”
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Activities of Tetramethylene-Bis-Onium Reversible Cholinesterase Inhibitors as Influenced by the Nature of the Onium Atom by Basova, N. E., Kormilitsyn, B. N., Perchenok, A. Yu, Rozengart, E. V., Saakov, V. S., Suvorov, A. A.

“…Inorganic tetramethylene bis -onium compounds were studied as reversible inhibitors of various cholinesterases (ChE), i.e., human erythrocyte acetyl-ChE, horse…”
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Ligands of cholinesterases of ephedrine and pseudoephedrine structure by Basova, N E, Kormilitsin, B N, Perchenok, A Yu, Rozengatt, E V, Saakov, V S, Suvorov, A A

“…The paper is a review of literature data on interaction of the mammalian erythrocyte acetylcholinesterase and blood serum butyrylcholinesterase with a group of…”
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Inhibitory effect of benzimidazole derivatives on cholinesterases of animals in the presence of different substrates by Basova, N E, Kormilitsyn, B N, Perchenok, A Iu, Rosengart, E V, Saakov, V S, Suvorov, A A

“…Specifically synthesized group of benzimidazole derivatives possessing varying degrees of delocalization of the positive charge in the cation group of the…”
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Lupinine and epilupinine derivatives as substrates of Mammalian cholinesterases by Basova, N. E., Kormilitsyn, B. N., Perchenok, A. Yu, Rozengart, E. V., Saakov, V. S., Suvorov, A. A.

“…Two series of lupinine and epilupinine acetates, the free bases and the N -methyl, N -ethyl, and N -propyl derivatives, were studied. Enzymatic hydrolysis of…”
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