[Optimization of protein hydrolysis by Bacillus subtilis alkaline proteinase]. / Optimizatsiia gidroliza belkov shchelochnoi proteinazoi Bacillus subtilis.

Casein hydrolysis by alkaline proteinase from Bacillus subtilis str. 72 had been investigated. It has been shown that the hydrolytic rate depends on the substrate concentration and declines rapidly with time even at low protein concentrations. It has been suggested to use an equation describing the time dependence of the rate of casein proteolysis and characterizing the optimum time of protein hydrolysis, maximum rate of hydrolysis, and the maximum yield of the reaction products.

[Effect of alcohols on the rate of cholinesterase decarbamoylation]. / Vliianie spirtov na skorost' dekarbamoilirovaniia kholinesterazy

Butanol-1 and butandiol-1,4 are shown to increase the decarbamoylation rate of N-methylcarbamoyl- and N,N-dimethylcarbamoyl-cholinesterase. It is mainly due to the formation of a ternary complex NEA which is decomposed in 2,5 times faster than corbamoyl-enzyme EA. This is an evidence for the presence of some allosteric center in cholinesterase which is capable of binding alcohols.

[Effect of nucleophiles on the conversion of choline esters under the action of cholinesterase]. / Vliianie nukleofilov na prevrashchenie kholinovykh éfirov pod deistviem kholinésterazy

It is shown that effect of alcohols ROH on the hydrolysis of butyryl-choline and acetylcholine by choline esterase (E. C. 3.1.1.8) is complex; it included the concurrent and the unconcurrent inhibitions, the interaction with the acylenzyme to form more reactive triple complex, and the acyl migration. By titrometric method it is found that proportion of the transacylation and hydrolysis rates depends on hydrophobity of R only being independent on its electronegativity.