V N Nikandrov

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Specific activity of streptokinase was decreased after incubation in the system containing I-ethyl-3(3-dimethyl aminopropyl) carbodiimide (EDC)--ethylene diamine. Under these conditions about 8 free amino groups and 38 free carboxylic groups were modified in the streptokinase molecule. The protein conformation and the state of tryptophane residues were(More)
It is established fact, that SK-initiated fibrinolysis is decelerated, when oxygen is removed from solutions; that SK possesses superoxide dismutase-like activity and that its activating function is sharply inhibited by superoxide radical scavengers. The point in discussion is the possibility of oxygen-dependent Pg activation, which is not related to(More)
The interaction of streptokinase with diethylpyrocarbonate resulting in partial inactivation of the protein was studied. Eight histidine residues are blocked per streptokinase molecule by this reagent. Ethoxyformylation of streptokinase histidyls is characterized by a rate constant corresponding to modification of free L-histidine. No reactivation of(More)
The rabbits with CCl4-induced hepatic failure have revealed changes in hemostasis responses to streptokinase administration. The main distinction of hepatic dystrophy was the depression of plasma fibrinolytic activity accompanying the decrease in fibrinogen and antiplasmin concentrations. Streptokinase administration to rabbits with productive inflammatory(More)
Modification of tyrosine residues was detected in streptokinase molecule during iodination. A nonlinear type of the modification reaction allowed to suppose that tyrosine residues were heterogenous. As shown by gel chromatography the modified streptokinase did not develop stable complexes with human plasminogen even at low ratios of iodine/streptokinase,(More)
The dynamic study of the protein spectrum of culture fluid during the growth of beta-hemolytic streptococcal strain H46A has been carried out by the methods of electrophoresis and isoelectrofocusing in polyacrylamide gel. Changes in the protein spectrum have phasic character and, on the whole, reflect the state of the microbial population, the presence of(More)
We showed, using the method of lysis of fibrin plates and five substrate proteins in a thin layer of agar gel, that inorganic orthophosphate (0.001-0.06 M) enhances by 50-250% the activatory functions of streptokinase, urokinase, and tissue plasminogen activator and, in general, by 1.2-12.0 times enhances protein lysis by trypsin, alpha-chymotrypsin,(More)
Scavengers of different active oxygen species affect fibrin plate lysis, catalysed by various proteinases, only at relatively high concentrations (> 10(-2) M). Singlet oxygen scavengers change proteinase activity insignificantly except for strong inhibition of pepsin and papain by sodium azide, but pepsin-by histidine, and fibrinolytic urokinase activity-by(More)