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L P Kuznetsova

Publications and source records attributed to L P Kuznetsova.

At least 19 recordsLinked to original sources
PubMed2001

[The inhibition enzymatic hydrolysis of acetylthiocholine by acetylcholinesterase using principal alkaloids isolated from celandine and macleya and their derivatives].

A study was made of a possible inhibitory action on the enzymatic hydrolysis of acetylthiocholine by human erythrocyte acetylcholinesterase of principal alkaloids isolated from Chelidonium majus L. and Macleaya (Bocconia) cordata and microcarpa (namely sanguinarine, chelidonine, berberine), and of drugs "Ukrain" (thiophosphoric acid derivative of a sum of the alkaloids isolated from Chelidonium majus L.) and "Sanguirythrine" (a mixture of unseparated closely related to benzo[c]phenanthridine alkaloids sanguinarine and chelerythrine, isolated from Chelidonium majus L. and other plants of Papaveraceae family). All agents under study have been shown to be reversible inhibitors of the enzymatic hydrolysis of acetylthiocholine. On the basis of the kinetic data it has been determined that chelidonine belonged to reversible inhibitors of a competitive type. All other examined agents have been demonstrated to be inhibitors of a mixed competitive-noncompetitive type, and a greater contribution to the inhibition was made by the competitive constituent. Among all examined agents berberine, sanguinarine and "Sanguirythrine" were the strongest inhibitors of this reaction (the values of generalized inhibitory constants being 0.23, 0.23 and 0.29 microM, respectively) and cheliodonine and "Ukrain" were much weaker (2.0 and 2.5 microM, respectively). Judging from the data obtained, sanguinarine and chelerythrine exert similar inhibitory effects on the reaction of enzymatic hydrolysis of acetylthiocholine, since sanguinarine and "Sanguirythrine" have nearly equal generalized inhibitory constants.

Acetylcholinesterase↗
PubMed1996

[Features of inhibiting butyrylcholinesterase and carboxylesterase hydrolysis with fluoranhydride esters of beta,beta-diphenylethylphosphonic acid].

A new type of organophosphorus compounds-beta, beta-diphenylethylphosphonic acid fluoroanhydride esters-with various alkyl radicals (CH3, C2H5, C3H7, i-C3H7, C4H9, i-C4H9, C5H11, C6H13) and a phenyl radical (C6H5) have been tested as inhibitors of horse serum butyryl cholinesterase (EC 3.1.1.8) and two forms of reindeer liver carboxyl esterase (EC 3.1.1.1). All the tested compounds are strong irreversible inhibitors of butyryl cholinesterase and strong combined type inhibitors of carboxylesterase. The values of inhibitory constants have been found to depend on the structure of the alkyl radical in the inhibitor molecule.

Anhydrides↗
PubMedDate not supplied

[Method for determining nitrogen-containing cationic surface-active agents using butyrylcholinesterase].

The biochemical method for determination of cetyltrimethyl ammonium or cetylpyridinium, both being nitrogenated cationic surfactants, has been devised by using horse blood serum butyrylcholinesterase as analytical reagent. The method streams from the fact that surfactants tested are inhibitors of butyrylcholinesterase hydrolysis of butyrylcholin, a cationic substrate, but in this case they activate enzymatic hydrolysis of 1-naphthylacetate, a neutral substrate. Presence two opposite effects enlarges reliability to identifications. Use the sensitive fluorimetric method to registrations of activation of hydrolysis a substrate 1-naphtylacetate vastly to reduce the threshold of determination of surfactants above.

Animals↗
PubMedDate not supplied

[Use of 1- and 2-thionaphthylacetates as cholinesterase substrates].

1- and 2-thionaphthylacetates were tested as cholinesterase substrates. It was shown that the butyrilcholinesterase from horse serum can hydrolize these compounds. The hydrolysis velocity of 1-thionaphthylacetate was comparable with hydrolysis velocity of acetylthiocholine (the well known cholinesterase substrate), but 2-thionaphthylacetate was hydrolysed more slowly. The values of the kinetic parameters V and K(m) for butyrylcholinesterase hydrolysis of 1- and 2-thionaphthylacetates were determined. It was offered to use 1-thionaphthylacetates as the substrate for cholinesterases.

Acetylthiocholine↗
PubMedDate not supplied

[Comparative study of enzymatic activity of cholinesterases of different origin in thionaphthylacetate hydrolysis reactions].

A comparative determination of kinetic parameters V and Km in the reaction of hydrolysis thionaphthylacetate and well known substrate acetylthiocholine by choline esterases from different sources was conducted. It is shown that butyrylcholine esterases hydrolyze thionaphthylacetate with velocity comparable with that of hydrolysis of acetylthiocholine, while acetylcholine esterases and propionylcholine esterases hydrolyze this substrate several times slower than acetylthiocholine. The values of Km in the reactions of hydrolysis of thionaphthylacetate for all studied cholinesterases is an order higher than for acetylthiocholine except cholinesterase of blood serum of fish. This value for the latter enzyme is practically equal.

Acetylthiocholine↗
PubMedDate not supplied

[Effect of some isoquinoline alkaloids on enzymatic activity of acetylcholinesterase and monoamine oxidase].

It has been shown, that some benzo[c]-phenanthridine and diisoquinoline alkaloids isolated from Chelidonium majus L. and Macleaya (Bocconia) cordata and M. microcarpa (berberine, sanguinarine, chelidonine) and of drugs ("Ukrain" and "Sanguirythrine") inhibited the enzyme activity of acetylcholinesterase from human erythrocyte and monoamine oxidase from the rat liver. All agents under study have been shown to be reversible inhibitors of the enzymatic hydrolysis of acetylthiocholine. It has been determined that chelidonine belonged to reversible inhibitors of a competitive type, all other examined agents have been demonstrated to be inhibitors of a mixed competitive-noncompetitive type, and a greater contribution to the inhibition was made by the competitive constituent. Among all examined agents berberine, sanguinarine and "Sanguirythrine" were the strongest inhibitors of this reaction and chelidonine and "Ukrain" were much weaker. All agents under study have been shown to be irreversible inhibitors of the oxidative deamination reaction of serotonine and tyramine and not to influence the oxidative deamination reaction of benzylamine as a substrate. Among the examined agents, alkaloid sanguinarine and drug "Ukrain" are the strongest inhibitors of the reaction, alkaloids berberine, sanguinarine and "Sanguirythrine" exhibit a weaker action.

Acetylcholinesterase↗
PubMedDate not supplied

[Influence of the substrate nature, ethanol and phosphate buffer on the butyrylcholinesterase hydrolysis retardation by reversible inhibitors].

The reversible inhibition of horse blood serum butyrylcholinesterase (Ce 3.1.1.8) hydrolysis of ion substrates of acetyl- and butyrylthiocholines and non-ion substrate of indophenylacetate by N-methyl-4-piperidinylbenzylate and tacrine (1,2,3,4,-tetrahydro-9-aminoacridine) and phosphate buffer and ethanol influence on this process are investigated. The values of competitive Ki, uncompetitive K'i and generalized K sigma inhibitory constants are determined. It is shown that the inhibition effect and reversible inhibition type depend not only on the inhibitor and substrate nature but also on the phosphate buffer concentration and ethanol presence in the reaction mixture.

Buffers↗
PubMedDate not supplied

[Catalytic properties of cholinesterases immobilized in a gelatin membrane].

Catalytic properties of human blood erythrocyte acetylcholinesterase and horse blood serum butyrylcholinesterase immobilized and nonimmobilized in the gelatin membrane have been comparatively studied. Cholinesterase immobilization induces an increase in the Michaelis constant value and a decrease in the maximum rate value in reactions of enzymic hydrolysis of thiocholine ethers, but exerts no effect on these kinetic parameters in case of enzymic hydrolysis of indophenylacetate. The effect of reversible inhibitors: galanthamine, N-methyl-4-piperidinyl benzylate and 1,2,3,4-tetrahydro-9-aminoacridine (tacrine), as well as of irreversible inhibitors: O-ethyl-O-(4-nitrophenyl)ethyl phosphonate (armin), diisopropyl fluorophosphate (DFP), O,O-diethyl-O-(4-nitrophenyl) phosphate (paraoxon) and O,O-dimethyl-O-(2,2-dichlorovinyl) phosphate (DDVP) on immobilized cholinesterases is weaker as compared with the effect on nonimmobilized enzymes. The results obtained are discussed for the effect of immobilization on the catalytically active enzyme surface.

Acetylcholinesterase↗
PubMedDate not supplied

[Effect of salt composition of the medium and ethanol on cholinesterase hydrolysis of various substrates].

Sodium chloride, phosphate buffer and ethanol were studied for their effect on butyryl cholinesterase hydrolysis rate of acetylcholine, acetylthiocholine, butyrylthiocholine and nonion substrate of indophenylacetate. The concentrations of 1.10(-2) = 1.10(-1) M of sodium chloride activated enzymatic hydrolysis of ion substrates at the concentrations lower than 1.10(-4) M but sodium chloride is a competitive inhibitor at higher concentrations. Phosphate buffer also activates substrates enzyme hydrolysis at the concentrations of 2.10(-4) M and lower, but it inhibits incompetitively the nonion substrate indophenylacetate hydrolysis. Ethanol activates butyrylthiocholine hydrolysis and is a competitive inhibitor in acetylthiocholine and indophenylacetate hydrolysis. The observed effects are discussed on the assumption of two forms of butyrylcholinesterase E' and E" existence. These two forms are determined by different kinetic parameters and are in equilibrium.

Animals↗
PubMedDate not supplied

[A kinetic study of the blood serum cholinesterase activity in the freshwater fish Abramis ballerus].

In reaction of hydrolysis of choline and thiocholine esters of carbonic acids at 25 degrees C, cholinesterase activity of the blood serum from the fish A. ballerus has been studied by modified Ellman's method and potentiometric titration method. The activity is maximal in pH region 7.5-9.0 and is not inhibited by high concentration of substrates. Michaelis constants and maximal rates for the enzyme reactions were determined. Butyrylcholine and butyrylthiocholine were hydrolyzed with the highest rates by the serum. Some of the organophosphorus inhibitors (diisopropylfluorphosphate and DDVF) inhibit cholinesterase activity of the blood serum significantly faster, whereas some of the carbamates (aminostygmin, eserine, etc.) inhibit it significantly slower than typical butyrylcholinesterase from horse blood serum and typical acetylcholinesterase of human erythrocytes. Besides, with respect to the sensitivity to inhibitors and some other properties, fish blood serum cholinesterase differs from other known cholinesterases.

Acetylcholinesterase↗