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Effect of Ethanol on The Enzyme-Substrate Interaction of Dehydrogenases
The analysis of published data showed the necessity and urgency of research of theinteraction specificity of small and large molecules that might have a regulatory value. In in vitro conditions we were studying the effect of ethanol on the activity of dehydrogenases: glyceraldehyde phosphate dehydrogenase -GAPDH (EU 1.2.1.12), α-glycerol phosphate dehydrogenase -α-GPD(EU 1.1.1.8) and lactate dehydrogenase -LDH (EU 1.1.1.27) -in the hemolysate of red blood cells and in the isolated homogeneous enzymes. A comparative evaluation of enzyme activity after their incubation with ethanol in the hemolysate and in the isolated environment showed that the activity of GAPDH, α-GPDand LDH increased in both media, but in a quantitative ratio the enzyme activity in isolated the environment was considerably smaller than in the hemolysate -multicomponent medium. Thus, during the metabolic adaptation to the effect of external stimulus the efficiency of all studied dehydrogenases increases. Ethanol can play the role of regulator of molecular processes of metabolism by modulating the enzyme-substrate interaction.