[Production of fibrous materials, containing an immobilized proteolytic enzyme and urea]. / Poluchenie voloknistykh materialov, soderzhashchikh immobilizovannyi proteolitichskii ferment i mochevinu.

Immobilization of cellulose and polyacrylic acid on a grafted copolymer increased significantly the stability of proteolytic enzymes to inactivation by urea. Materials containing immobilized proteolytic enzymes and urea and displaying a combined biological activity were obtained.

[Coimmobilization on unmodified polymers of the proteolytic enzyme protease S and antimicrobial drugs]. / Issledovanie sovmestnoi immobilizatsii na nemodifitsirovannykh polimerakh proteoliticheskogo fermenta proteazy S i antimikrobnykh preparatov.

In order to develop materials of prolonged biological effects, the proteolytic enzyme protease S was coimmobilized with antimicrobial drugs chlorhexidine bigluconate and gentamicin sulfate on unmodified cellulose and polyester fibrous materials. The drugs were incorporated into the polymeric composition, which was attached to the materials studied.

[Coimmobilization of proteolytic and bacteriolytic enzymes and properties of isolated materials]. / Issledovanie sovmestnoi immobilizatsii proteoliticheskogo i bakterioliticheskogo fermentov i svoistv poluchennykh materialov.

Coimmobilization of proteolytic and bacteriolytic enzymes on a carboxyl-containing grafted cellulose copolymer was studied. The resistance of lysozyme to gamma-sterilization significantly increased after coimmobilization with a proteolytic enzyme. The resulting material accelerated the cleansing of wounds.

[Preparation of films with combined biological activity and study of their properties]. / Poluchenie plenok s kombinirovannym biologicheskim deistviem i issledovanie ikh svoistv.

Joint immobilization of a proteolytic enzyme (terrilytin, protease C, or collytin) and an antimicrobial compound or the bacteriolytic enzyme lysozyme in the structure of polyvinyl alcohol was studied. Changes in the activity of immobilized enzymes upon x-ray sterilization were studied. These materials were highly effective in wound healing.

[Preparation of fiber materials containing both the immobilized proteolytic enzyme and antimicrobial substance, and study of their properties]. / Poluchenie voloknistykh materialov, soderzhashchikh odnovremenno immobilizirovannyi proteoliticheskii ferment i antimikrobnoe veshchestvo, i issledovanie ikh svoistv.

Properties of joint immobilization of a proteolytic enzyme (terrilytin, trypsin, collytin, or protease C) and an anti-microbe compound to cellulose copolymer containing carboxyl groups were investigated. It was established that the molecule of anti-microbe substance containing a few base groups enhanced stability of the enzyme immobilized, most likely due to additional fixation of the enzyme macromolecule. Changes in activity of the materials containing both protease and anti-microbe compound were studied upon gamma-sterilization and subsequent prolonged storage. The materials with combined biological action were demonstrated to accelerate markedly wound cleansing and healing.

[Rational organization of the technological processes of hydrolyzing whey lactose in the presence of a heterogeneous fiber biocatalyzer]. / Ratsional'naia organizatsiia tekhnologicheskogo protessa gidroliza laktozy molochnoi syvorotki v prisutstvii geterogennogo voloknistogo biokatalizatora.

We have studied lactose hydrolysis in whey in the presence of a fibrous biocatalyst containing immobilized beta-galactosidase in a continuous-flow column reactor, and in a reactor unit with substrate recycling in batch and continuous regimes. The comparative study of the efficiency of the reactors allowed us to recommend the reactor unit with substrate recycling for lactose hydrolysis in whey in the batch regime, since it provides both satisfactory hydrodynamic stability and high productivity.

[Antimicrobial x-ray contrast articles]. / Antimikrobnye rentgenokontrastnye izdeliia.

A procedure has been developed to prepare the radio-opaque polymer composition containing an antimicrobial substance that can be used in medicine. The findings of the antimicrobial activity of products made of the above composition are presented in the paper.

[Preparation of porous material based on alginic acid, containing immobilized terrilytin]. / Poluchenie poristogo materiala na osnove al'ginovoi kisloty, soderzhashchei immobilizovannyi terrilitin.

A comparative study was conducted on immobilization of terrilytin on alginic acid by attaching the enzyme by ionic or covalent bonds and possible use of such compounds in preparing porous coatings for wound treatment. It was shown possible to prepare a coating with the enzyme activity after radiation sterilization equal to 80-85 per cent of the initial level. Medico-biological investigations proved that the use of the coating in treatment of purulent wounds was efficient.

[Effect of the structure of polymeric materials on the properties of immobilized enzymes]. / Vliianie struktury polimernykh materialov na svoistva immobilizovannykh v nikh fermentov.

The relationship between the structure of triacetate cellulose fibres and films and properties of enzymes entrapped in these materials was investigated. Trypsin and penicillin amidase were entrapped in triacetate cellulose films and fibres during their formation. The effect of permeability of the films on the catalytic properties of entrapped trypsin was studied. The porous structure of triacetate cellulose fibres with entrapped penicillin amidase was studied, the fibres being produced by different methods. An increase of porosity and the specific surface of the fibre-biocatalyst reduced the Km value and the energy of activation of the hydrolytic decomposing of benzyl penicillin but increased the Vmax value.

[Preparation of films and fibers containing proteolytic enzymes]. / Poluchenie plenok i volokon, soderzhashchikh proteoliticheskie fermenty.

Immobilization of the proteolytic enzymes trypsin and terrylitin in fluorplastic-42 films and fibers as well as in water-soluble polymeric (polyvinyl alcohol and carboxymethyl cellulose) films was being studied during preparation of the films. The properties of the proteolytic enzymes immobilized in the polymers are dependent on the conditions of preparation of fibers and films.

[Experimental and clinical use of various forms of immobilized proteinases and their inhibitors]. / Opyt éksperimental'nogo i klinicheskogo ispol'zovaniia v meditsine razlichnykh form immobilizovannykh proteinaz i ikh ingibitorov.

Analysis of the data obtained in experimental (971 animals) and clinical (250 patients) studies with various immobilized proteinases and their inhibitors showed that this approach to enzymotherapy is a perspective one. Immobilized enzymes and inhibitors exceeded distinctly the native preparations in therapeutic efficiency and were devoid of their disadvantages (low stability and autolysis of proteinases, inactivation by inhibitors, occurring in blood and tissues, rapid elimination of the inhibitors from the organism). Wide use of immobilized enzymes and inhibitors in medical practice offered new possibilities in surgery, shortened distinctly the duration of patients treatment and enabled to decrease the doses of drugs and consumption of dressing materials.

[Immobilization of modified alpha-chymotrypsin within the structure of cellulose triacetate membranes]. / Immobilizatsiia midifitsirovannogo al'fa-khimotripsina v strukture plenok iz tritsetata tselliulozy.

Immobilization of alpha-chymotrypsin on carboxymethyl esters of dextran (mol. weights of 60 000 and 100 000), whose macromolecules contain 2-amino-4-chloro-s-triazine residues, results in water-soluble polymeric derivatives of alpha-chymotrypsin, containing up to 60% of the enzyme. The activity of the immobilized enzyme makes up to 90% of the initial one. Using dextran blue as a matrix, a polymeric derivative of alpha-chymotrypsin, containing 9% of a chemically bound enzyme, which retains 20% of its initial activity, has been obtained in a similar way. The thermal stability of the enzyme increases during alpha-chymotrypsin linking to carmoxymethyl esters of dextran. The incorporation of alpha-chymotrypsin into the triacetate cellulose membrane (CTA) during its formation results in a practically complete desorption of the enzyme from the membrane into 1 M NaCl. During incorporation of alpha-chymotrypsin linked to the carboxymethyl ester of dextran (mol. weight 60 000) into the CTA membrane the bulk of the modified enzyme is desorbed, whereas in the case of alpha-chymotrypsin linked to the carboxymethyl ester of dextran with mol. weight of 100 000 or to the blue dextran only an insignificant part of the enzyme is desorbed. The thermal stability of alpha-chymotrypsin and the labile form of the enzyme linked to the carboxymethyl ester of dextran with mol. weight of 100 000 increases during the enzyme incorporation into the CTA membrane.

[E. coli penicillin amidase. Physico-chemical properties of the enzyme covalently bound to the 2-(3'-amino-4'-methoxyphenyl)-sulfonylethyl ester of cellulose]. / Penitsillinamidaza iz E. coli. Nekotorye fiziko-khimicheskie svoistva fermenta, kovalentno sviazannogo s 2-(3'-amino-4'-metoksifenil)-sul'fonilétilovym éfirom tselliulozy.

The effect of the procedure of the enzyme binding with the carrier on the properties of the heterogenous catalyst obtained by covalent binding of penicillinamidase (PA) with cellulose 2-(3'-amino-4'-methoxyphenyl)-sulphonylethyl ether by means of the bifunctional reagent, i.e. glutaric aldehyde was studied. It was shown that the amount of the bound enzyme increased with a rise in the amount of the enzyme taken for the binding, while the binding efficiency characterizing the part of the active enzyme in the total amount of the bound PA decreased practically 2 times. The use of the enzyme preparations with different purify levels for the binding provided differentiation of the effects resulting in the activity loss on immobilization. In other words it provided separate estimation of the inactivation effect of the matrix and the immobilization procedure, as well as the interaction of the enzyme molecules with each other and other protein molecules.

[Properties of urease immobilized by chemical binding to a derivatives of cellulose]. / Issledovanie svoistv ureazy, immobilizovannoi putem khimicheskogo prisoedineniia k proizvodnym tselliulozy.

A comparative study of properties of soluble urease and urease immobilized by its binding to cellulose derivatives was carried out. Upon chemical binding of urease to cellulose derivatives the Mikhaelis constant and pH optimum for the enzyme action changed insignificantly. Maximum enzymic activity of soluble and immobilized urease occurred at 50 degrees C. The energy of activation of urea hydrolysis by urease during enzyme immobilization also changed insignificantly.

[Modification of the properties of drugs combined with polymers. II]. / Modifikatsiia svoistv lekarstvennykh veshchestv putem prisoedineniia ikh k polimeram. Chast' II.

In the second part of the paper there have been discussed the works on modification of drugs properties when coupled with polymers in terms of covalent links. It was proved on a number of cases that chemical bonds of specified drugs and polymers allows to increase the durability and effective action of these remedies, to decrease the toxicity, to increase the solubility and immunity against ferments and, moreover, enable the advantageous disposal of these substances in particular organs.

[Modification of properties of drugs combined with polymers. I]. / Modifikatsiia svoistv lekarstvennykh veshchestv putem prisoedineniia ikh k polimeram. Chast' I

The article reviews the papers on modifying the properties of drugs by their administration in the form of a mixture with polymers, or combination of the drugs and polymers using coordinative or ionic bonds. In many cases the combination of drugs and polymers by chemical means or preparation of a mixture of drugs and polymers prolongs and increases the effectivity of drugs, increases their solubility, decreases their toxicity, and modifies their distribution in the organs.

[Properties of penicillin amidase covalently bound to cellulose matrices]. / Svoistva penitsillinamidazy, kovalentno sviazannoi s tselliuloznymi matritsami

Properties of penicillinamidase (PA) covalently bound with the cellulose matrix were studied. The efficiency of the binding depended on the bind type and purity of the native enzyme taken for binding. Stability of the immobilized PA (IPA) was studied at wide pH ranges. The effect of the ion strength, substrate concentration and purity of the native PA on stability of IPA was also investigated. The maximum stability of the enzyme was observed at pH 6.5-7.0 Stability of IPA depended on the purity of the native enzyme. When PA of the diazotized ether of cellulose containing amino groups was used, the enzyme was destabilized. IPA prepared on chlortriazinylcellulose was more stable than the respective native PA almost by I order.