The effect of ethanol on protein-ligand interactions

The relevance of studying the regulation of protein-ligand interactions is due to the emergence of new views on the role of metabolites and their key importance in vital processes. To study the protein-ligand interaction, the AB0 antigen-antibody blood system and the enzyme-substrate system of dehydrogenases were used as a test system, and ethanol was used as an influencing factor. In experiments performed with A and B blood erythrocyte antigens, natural AB0 system antibodies and monoclonal antibodies under the influence of ethanol performed change of the degree of agglutination and the time to onset of erythrocyte agglutination. It was found that ethanol can regulate the enzyme-substrate interactions of dehydrogenases: lactate dehydrogenase (EC 1.1.1.27), glyceraldehyde phosphate dehydrogenase (EC 1.1.1.12), and α-glycerol phosphate dehydrogenase (EC 1.1.1.8). The increase in the activity of studied enzymes under the influence of ethanol in the whole blood hemolysate was 2.5 - 3 times higher than in the isolated medium (with pure enzyme preparations). © Published under licence by IOP Publishing Ltd.

Authors
Ryskina E.A. 1 , Gilmiyarova F.N. 2 , Ahmedzhanov B.B. 3 , Maksimuk N.N.4
Publisher
Institute of Physics Publishing
Number of issue
3
Language
English
Status
Published
Number
032111
Volume
677
Year
2021
Organizations
  • 1 Higher School of Economics (HSE University), Moscow, Russian Federation
  • 2 Samara State Medical University (SamSMU University), Samara, Russian Federation
  • 3 Peoples' Friendship University of Russia (RUDN University), Moscow, Russian Federation
  • 4 Novgorodskiy Gosudarstvennyy Universitet Imeni Yaroslava Mudrogo (NovSU), Veliky Novgorod, Russian Federation
Keywords
Antigen-antibody reactions; Antigens; Bacteria; Biotechnology; Enzymes; Ethanol; Ligands; Metabolites; Monoclonal antibodies; Blood erythrocytes; Blood system; Enzyme preparation; Enzyme substrates; Enzyme-substrate interactions; Glycerol phosphate; Lactate dehydrogenase; Protein-ligand interactions; Blood
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