Published in Biokhimiia on March 01, 1977
Micellar enzymology. Eur J Biochem (1986) 1.26
The mechanochemistry of immobilized enzymes. How to steer a chemical process at the molecular level by a mechanical device. Biochim Biophys Acta (1974) 1.19
The principles of enzyme stabilization. VI. Catalysis by water-soluble enzymes entrapped into reversed micelles of surfactants in organic solvents. Biochim Biophys Acta (1981) 1.12
Substrate specificity of penicillin amidase from E. coli. Biochim Biophys Acta (1980) 1.08
[Use of integrated rate equations for the determination of the kinetic constants of enzyme reactions]. Biokhimiia (1972) 1.06
The role of entropy and enthalpy factors in kinetic specificity of -chymotrypsin. Temperature dependence study of acyl- -chymotrypsins deacylation. Biochim Biophys Acta (1972) 1.03
[Kinetic study of o-dianisidine oxidation by hydrogen peroxide in the presence of horseradish peroxidase]. Biokhimiia (1977) 1.03
The principles of enzyme stabilization. I. Increase in thermostability of enzymes covalently bound to a complementary surface of a polymer support in a multipoint fashion. Biochim Biophys Acta (1977) 1.02
Structure-stability relationship in proteins: fundamental tasks and strategy for the development of stabilized enzyme catalysts for biotechnology. CRC Crit Rev Biochem (1988) 0.93
NAD-dependent formate dehydrogenase from methylotrophic bacterium, strain 1. Purification and characterization. Eur J Biochem (1979) 0.91
Catalysis by enzymes entrapped into hydrated surfactant aggregates having lamellar or cylindrical (hexagonal) or ball-shaped (cubic) structure in organic solvents. Eur J Biochem (1986) 0.90
[New approach to the study of enzyme reactions with the participation of water-insoluble substrates. Pancreatic lipase incorporated into the inverted micelles of a surface-active substance in an organic solvent]. Dokl Akad Nauk SSSR (1983) 0.88
[Inhibition of cathepsin G and elastase from human granulocytes by multiple forms of the Bowman-Birk type of soy inhibitor]. Biokhimiia (1993) 0.88
[Inhibition of glucose isomerase from Actinomyces olivocinereus 154 by polyols]. Biokhimiia (1980) 0.86
Chemical modification of the epsilon-amino groups of lysine residues in horseradish peroxidase and its effect on the catalytic properties and thermostability of the enzyme. Biochim Biophys Acta (1979) 0.84
The principles of enzyme stabilization. II. Increase in the thermostability of enzymes as a result of multipoint noncovalent interaction with a polymeric support. Biochim Biophys Acta (1977) 0.84
The principles of enzyme stabilization. IV. Modification of 'key' functional groups in the tertiary structure of proteins. Biochim Biophys Acta (1979) 0.84
Activity of antioxidant enzymes in the skin during surgical wounds. Bull Exp Biol Med (2006) 0.84
The protoporphyrin-apoperoxidase complex as a horseradish peroxidase analog. A fluorimetric study of the heme pocket. Biochim Biophys Acta (1981) 0.83
The reactions of alpha-chymotrypsin and related proteins with ester substrates in non-aqueous solvents. Eur J Biochem (1975) 0.83
[Bifunctional reversible inhibitors of proteolytic enzymes. Interaction between alpha-chymotrypsin and hexylboron acid]. Dokl Akad Nauk SSSR (1968) 0.83
[Micelle enzymology. The catalytic activity of peroxidase in a colloid solution of water in an organic solvent]. Dokl Akad Nauk SSSR (1983) 0.83
[Kinetics of fibrin lysis by plasmin: inhibition by fibrin degradation products]. Bioorg Khim (1996) 0.83
[Kinetics and mechanism of inactivation of isolated chloroplasts]. Mol Biol (Mosk) (1976) 0.82
[Enzymatic synthesis of 3,4-dihydroxyphenyl-L-alanine by free and immobilized Citrobacter freundii cells]. Prikl Biokhim Mikrobiol (1985) 0.82
[Cooxidation of potassium ferrocyanide and o-dianisidine by hydrogen peroxide catalyzed by horseradish peroxidase. Substrate-substrate activation]. Biokhimiia (1981) 0.81
Enzymatic mechanochemistry: a new approach to studying the mechanism of enzyme action. Biochim Biophys Acta (1976) 0.81
[Alcohol dehydrogenase substrate specificity in a colloidal solution of water in an organic solvent]. Dokl Akad Nauk SSSR (1982) 0.81
NAD+-dependent hydrogenase from the hydrogen oxidizing bacterium Alcaligenes eutrophus Z1. Stabilization against temperature and urea induced inactivation. Biochimie (1986) 0.80
Colloidal solution of water in organic solvents: a microheterogeneous medium for enzymatic reactions. Science (1982) 0.79
Artificial light-sensitive enzymatic systems as chemical amplifiers of weak light signals. Photochem Photobiol (1979) 0.79
[The classical Bowman-Birk soy inhibitor is an effective inhibitor of human granulocyte alpha-chymotrypsin and cathepsin G]. Biokhimiia (1994) 0.78
[Inhibition of elastin hydrolysis, catalyzed by human leukocyte elastase and cathepsin G, by the Bowman-Birk type soy inhibitor]. Biokhimiia (1994) 0.78
The interaction of amino acids with ophthaldialdehyde: a kinetic study and spectrophotometric assay of the reaction product. Anal Biochem (1980) 0.78
[Applicability of quantitative kinetic spectrophotometric method for glucose determination]. Biokhimiia (1977) 0.78
[Interaction of 4 active forms of trypsin with specific substrate and pancreatic inhibitor]. Biokhimiia (1971) 0.77
Comparative study of thermal degradation of electron transfer particle and reconstituted respiratory chain. Relation of electron transfer to reactivation of submitochondrial particles. Biochim Biophys Acta (1970) 0.77
[Catalytic properties and stability of horseradish peroxidase immobilized in polyacrylamide gel]. Biokhimiia (1976) 0.77
[Characterization of urokinase type plasminogen activator modified by phenylglyoxal]. Bioorg Khim (2002) 0.77
Kinetics of the inactivation of the protein-lipid complex, firefly luciferase, by sodium deoxycholate and its reactivation by phosphatidylcholine. Biochim Biophys Acta (1987) 0.77
[Conformation changes in bacterial formate dehydrogenase during complex-formation with cofactor and its analogs]. Dokl Akad Nauk SSSR (1986) 0.77
[Effect of immobilization on protein (trypsin) folding]. Mol Biol (Mosk) (1979) 0.77
[Kinetics of benzylpenicillin hydrolysis catalyzed by pencillin amidase]. Antibiotiki (1974) 0.77
[L-amino acid oxidases: properties and molecular mechanisms of action]. Biomed Khim (2013) 0.76
[NAD-dependent formate dehydrogenase from methylotrophic bacteria. Isolation and properties]. Biokhimiia (1977) 0.76
Study of the role of arginine residues in bacterial formate dehydrogenase. Biochim Biophys Acta (1981) 0.76
Light and ultrasonic regulation of alpha-chymotrypsin catalytic activity. Proflavin as a light- and sound-sensitive competitive inhibitor. FEBS Lett (1974) 0.76
[The role of histidine residues of formate dehydrogenase from Bacterium sp. 1]. Biokhimiia (1978) 0.76
[Phosphorescent immunoanalysis. Metalloporphyrins--an alternative to rare earth fluorescent measurements?]. Dokl Akad Nauk SSSR (1989) 0.76
Enzymatic synthesis in biphasic aqueous-organic systems. I. Chemical equilibrium shift. Biochim Biophys Acta (1981) 0.76
A new approach to preparative enzymatic synthesis. Biotechnol Bioeng (1977) 0.76
[Chemical modification of proteins (enzymes) by water-insoluble reagents]. Dokl Akad Nauk SSSR (1984) 0.75
[Photic initiation of low-molecular substrate hydrolysis during autocatalytic enzyme reproduction]. Dokl Akad Nauk SSSR (1974) 0.75
[Effect of chemical modification on thermal stability of horseradish peroxidase]. Biokhimiia (1977) 0.75
[Interaction of Pb2+ cations with the carboxyl group of the active center of trypsin and alpha-chymotrypsin proteolytic enzymes]. Dokl Akad Nauk SSSR (1971) 0.75
[Mechanochemistry of catalytic systems. Regulation by mechanical means of the enzymatic activity of trypsin immobilized in polyacrylamide gel]. Dokl Akad Nauk SSSR (1974) 0.75
[Some mechanisms of degradation and stabilization of the reconstructed respiratory chain of mitochondria in connection with the investigation of the mechanism of its formation]. Biokhimiia (1969) 0.75
[Kinetic manifestations of the active center structure of trypsin during inhibition of its enzymatic activity by Ag+ cations]. Biokhimiia (1971) 0.75
[Kinetics and mechanism of nucleophilic effect on the oxidation of o-dianisidine catalyzed by horseradish peroxidase]. Biokhimiia (1978) 0.75
[Kinetics and mechanism of action of horseradish peroxidase in the reaction of dioxyfumaric acid oxidation with atmospheric oxygen]. Biokhimiia (1976) 0.75
[Photooxidation of alpha-chymotrypsin in the presence of boric acid]. Dokl Akad Nauk SSSR (1970) 0.75
Noncovalent bonding of the competitive inhibitor -naphthol to -chymotrypsin. Mol Biol (1973) 0.75
[Effect of promotion on the kinetics of acetyl-alpha-chymotrysin solvolysis under the action of added nucleophilic agents]. Biokhimiia (1975) 0.75
[Chemical modification of epsilon-NH2 groups of lysine residues in horseradish peroxidase. Accessibility of these groups to different modifying agents]. Biokhimiia (1978) 0.75
[Enzymatic antibiotic synthesis. Study of the hydrolysis--synthesis of cephalothin reaction catalyzed by penicillin amidase]. Dokl Akad Nauk SSSR (1977) 0.75
[Stability of the hydrogenase of Thiocapsa roseopersicina phototrophic bacteria]. Dokl Akad Nauk SSSR (1975) 0.75
[Kinetic characteristics of the aspartate aminotransferase reaction catalyzed by free Escherichia coli cells]. Dokl Akad Nauk SSSR (1978) 0.75
[Initiation of autoactivation of trypsinogen using light-sensitive trans-n-(N,N,N-trimethylamino)-cinnamoyltrypsin]. Biokhimiia (1974) 0.75
[Administration of immobilized firefly luciferase for quantitative estimation of ATP and enzymes synthesizing and destroying ATP]. Biokhimiia (1978) 0.75
Denaturing agents (urea, acrylamide) protect enzymes against irreversible thermoinactivation: a study with native and immobilized alpha-chymotrypsin and trypsin. FEBS Lett (1975) 0.75
[Study of the penicillin amidase from E. coli. An ultrasonic method of studying the ph- and temperature-conformational transitions in the active center of the enzyme]. Antibiotiki (1976) 0.75
Kinetics and mechanism of complex formation with the active sites of alpha-chymotrypsin of the intermediate particle of the photochromic transformation of 2-(2',4'-dinitrobenzyl)-pyridine. Mol Biol (1974) 0.75
The principles of enzyme stabilization. III. The effect of the length of intra-molecular cross-linkages on thermostability of enzymes. Biochim Biophys Acta (1978) 0.75
[Reversible inactivation of alpha-chymotrypsin during interaction of CuII and AgI metal cations with the imadazole group of the histidine residue in an active center]. Dokl Akad Nauk SSSR (1970) 0.75
[S-shape character of the relation of the initial reaction rate to substrate concentration during inhibition by N-acetyl-D-tryptophan of the hydrolysis of ethyl aceturate by alpha-chymotrypsin]. Biokhimiia (1971) 0.75
[Interaction of trypsin with a trypsin inhibitor from bovine colostrum]. Biokhimiia (1975) 0.75
[Formation of primary alcohols and palmitic acid in the microbiological oxidation of hexadecane]. Prikl Biokhim Mikrobiol (1976) 0.75
The mechanism of the alpha-chymotrypsin and trypsin-catalyzed hydrolysis of amides. Evidence for the participation of the active serine in the amidase activity of trypsin. Eur J Biochem (1973) 0.75
Kinetic regularities of the reversible influence of effector on a two-stage enzymatic reaction. Mol Biol (1973) 0.75
[Isolation and properties of human immunoglobulin-peroxidase complex]. Biokhimiia (1978) 0.75
[Kinetic role of complex formation in alpha-chymotrypsin catalysis]. Biokhimiia (1971) 0.75
[Basic principles of enzyme stabilization. Increase in heat stability of alpha-chymotrypsin during immobilization on polymethacrylic acid gel]. Dokl Akad Nauk SSSR (1976) 0.75
[Properties of alpha-chymotrypsin enclosed into polycarbonate microcapsules. Estimation of the diffusion effect]. Biokhimiia (1977) 0.75
[Protective effect of respiratory chain substrates on inactivation of mitochondrial electron transfer particles by proteolytic enzymes and cobra venom]. Biokhimiia (1970) 0.75
The effect of mechanical stretching of the myosin rod component (fragment LMMMM S-2) on the ATPase activity of myosin. Biochim Biophys Acta (1978) 0.75
[Temperature dependence of a complex formation between alpha-chymotrypsin active center and competive inhibitors--aliphatic compounds]. Biokhimiia (1971) 0.75
[Microenvironment of enzymes as 1 of the factors determining enzyme stability. Stabilization of soluble and immobilized horseradish peroxidase]. Dokl Akad Nauk SSSR (1975) 0.75
[Thermal inactivation of NAD-H2-oxidase]. Dokl Akad Nauk SSSR (1967) 0.75
[Effect of N-alkylimidazoles on oxidation of o-dianizidine catalyzed by horseradish peroxidase]. Biokhimiia (1978) 0.75
[Kinetics of "aging" of the photosynthetic apparatus of isolated chloroplasts]. Dokl Akad Nauk SSSR (1974) 0.75
[Kinetics of reactions in polyenzyme systems. III. Electron transport processes]. Mol Biol (Mosk) (1979) 0.75
[Action of ultrasonics on alpha-chymotrypsin. A new approach to the study of conformational changes (transitions) in the active centers of enzymes]. Biokhimiia (1975) 0.75
Interaction of alpha-chymotrypsin with N-cinnamoylimidazole. Substrate sensitive to light. Eur J Biochem (1971) 0.75
Effect of ionic strength of the steady-state kinetics of -chymotrypsin-catalyzed reactions. Mol Biol (1973) 0.75
[The protective effect of substrates under inactivation of NADH oxidase and succinate oxidase by cobra venom and trypsin]. Biokhimiia (1968) 0.75
[Kinetics of the hydrolysis reaction catalyzing alpha-chymotrypsin and trypsin in the presence of added nucleophilic agents]. Biokhimiia (1971) 0.75
[Kinetics and the mechanism of interaction of rhodamine 6G with the active center of alpha-chymotrypsin]. Mol Biol (1973) 0.75
Effect of substrates on reconstitution of the mitochondrial respiratory chain under various conditions. Biochim Biophys Acta (1969) 0.75