[Enzyme immobilization via silochromes, modified by transition metal salts].

The immobilization of pectoawamorine G 10X, pronase E and P, protease from Bac. mesentericus and rat liver microsomal fraction was performed by sylochromes modified by Ti, Zr and Hf salts. The pectinesterase, caseinolytic, esterase and hydroxylating activity of the immobilized preparations, their stability during storage, thermostability and pH optimum are determined.

[Immobilization of pectawamorine G10x by gel entrapment].

Polyacrylamide gel immobilization of pectawamorine G10x was investigated. Its pectinesterase and polygalacturonase activity and stability in storage were measured. The degree of pectawamorine binding during gel immobilization was 80--90%, 55% of initial activity being retained.

[Application of immobilized animal liver microsomal fraction to the reaction of 1,4-benzdiazepine-2-one conversion].

The albino rat strain Wistar and Shynashylla rabbit liver microsomal fraction was immobilized by incorporation into polyacrylamide gel. It is shown, that the microsomal fraction immobilized by such a method catalyzes the hydrolysis of 1,4-benzdiazepine-2 ones, 3-acetoxyderivatives, hydroxylation in position 3 of 1,4-benzdiazepine-2-ones and reduction of nitrazepame. The storage thermostability and stability of the immobilized preparations were studied.

[Study of the dynamics of fibrinolysis in a thin layer under the influence of streptokinase].

Dynamics of fibrinolysis in a thin layer of a fibrin-agar plate containing streptokinase undergoing the action of the blood plasma enzymes taken from a healthy person was examined. A continuous recording of the area covering the lysis zone was made. The fibrinolysis process on the fibrin-ager plate is shown to proceed uniformly.