[Supramolecular reorganizations in cellulose during hydration].

The analysis of modern ideas about the structural organization of the cellulose microfibrils is carried out. The mechanism of the formation of additional capillary-porous system of cellulose under moistening is offered. It is established that when the moisture content of cellulose reaches 8-10%, the filling of its micropores occurs with a simultaneous increase in their cross sizes, a specific surface and reduction in the degree of crystallinity of specimens.

[Inhibition of liver mitochondrial monoamine oxidase activity by alkaloids isolated from Chelidonium and Macleaya and by their derivative drugs].

It has been shown that the major alkaloids from plants Chelidonium majus L. and Macleaya (Bocconia) cordata and microcarpa, namely, berberine, sanguinarine, chelidonine, and drugs "Ukrain" (thiophosphoric acid derivative of a sum of the alkaloids isolated from Ch. majus L.

[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.

[A new method of preparing and some properties of high molecular weight monoamine oxidase from swine liver mitochondria].

Isolation of highly purified and highly molecular monoamine oxidase (MAO) from pig liver mitochondria have been worked out. Specific activity of isolated preparation is 2700 times higher than of original mitochondria homogenate. Enzyme solubilization by digitonin, affinity chromatography purification and ultrafiltration underlie this method.

[Amine oxidase from the bacterial strain Methanosarcina barkeri 27].

A new source of the enzyme amine oxidase (AO), namely bacteria of Methanosarcina barkery 27 strain, was discovered. The method AO isolation and purification from the bacteria was developed and the enzyme substrate and inhibitory specificity was studied. Contrary to some other microbial amine oxidases the AO investigated was shown to determine benzylamine and serotonin along with tyramine, all these substrates being deaminated at the equal rate.

[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.

[Catalytic properties of cholinesterases immobilized in N-phthalylchitosan and gelatin].

Catalytic properties of human blood erythrocyte acetylcholinesterase, horse blood serum butyrylcholinesterase and squid visual cholinesterase nonimmobilized and immobilized in N-phthalylchitozane and in gelatin have been comparatively studied. Immobilization of cholinesterases in N-phthalylchitozane does not change its catalytic properties in respect to substrates and inhibitors but increases the enzyme stability. Cholinesterase immobilization in the gelatin membrane increases the Michaelis constants and decreases the maximum velocities in the reaction of enzyme hydrolysis of thiocholine esters and (for squid visual ganglia cholinesterase) of indophenylacetate.

[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.

[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.

[Reactivation of phosphorylated cholinesterase immobilized in a gelatin membrane].

The soluble and immobilized cholinesterases (acetyl cholinesterase of human blood erythrocytes (EC 3.1.1.

[Stabilization of fly head cholinesterase immobilized on a gelatin membrane].

Immobilization of meat fly head cholinesterase in gelatin membrane essentially increases the enzyme stability and changes its kinetic characteristics: the Michaelis constant and maximum velocity of acetylthiocholine hydrolysis and also biomolecular velocity constant of phosphorylation by DDVP.

[Determination of the enzyme activity in tissue homogenates and biological liquids].

The described method for measuring the enzymic activities in tissue homogenates and biological fluids is based on the separation of the space with the biological fluid, where the enzymic reaction takes place, from the space with the substrate solution, where the analytical effect is measured, by a semipermeable membrane. The authors present the results of measurements of monoamine oxidase activity in rat liver mitochondria homogenate, of acetylcholinesterase activity in mouse brain homogenate, and of cholinesterase activity in cow blood serum.

[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.

[Comparative sensitivity of 2 carboxylesterases from the reindeer liver to various inhibitors].

The sensitivity to the inhibitor of two forms of reindeer liver carboxylesterases differing in electrophoretic mobility and conventionally termed as "slow" and "fast" forms were investigated. The rate constants for the interaction of organophosphorous irreversible inhibitors--diisopropylfluorophosphate (DPP) and two methylthiophosphonic acid thioesters--C5H11O(CH3)P(O)S(CH2)SCH2C(O)OCH3 (Sh-205) and, C8H17O(CH3)P(O)S(CH2)SCH2C(O)OCH2 (Sh-207)--with the "fast" form are hundreds of times as high as those with the "slow" one. The rate constants for irreversible carbamate inhibitor interaction byehone with both carboxylesterase forms were approximately equal to 1.

[The female climacteric and hypertension. An assessment of physical work capacity during treatment].

Bicycle ergometry was used for a study of physical working capacity in 114 women with hypertension, of them in 63 concomitant menopause was diagnosed. A noticeable decrease in physical working capacity and efficacy of functioning of the cardiovascular system during muscular work was demonstrated in patients with hypertension combined with menopause. An opportunity of restored tolerance to physical exercise in most of the patients with hypertension and in more than half of the patients with hypertension combined with menopause was shown during prolonged 6-month hypotensive therapy.