Interaction of ethanol with blood proteins

Alcohol Alcohol Suppl. 1987:1:283-7.

Abstract

At concentrations arising in alcohol intoxication ethanol was reversibly bound to human serum albumin and hemoglobin. Alcohol altered the conformation and stability of the proteins, reduced the domain-domain interactions in the molecule of albumin and changed the binding of such hydrophobic ligands as ANS and bilirubin.

MeSH terms

  • Bilirubin / metabolism
  • Blood Proteins / metabolism*
  • Ethanol / pharmacokinetics*
  • Ethanol / pharmacology
  • Hemoglobins / metabolism
  • Humans
  • Methemoglobin / metabolism
  • Oxyhemoglobins / metabolism
  • Protein Conformation / drug effects
  • Serum Albumin / metabolism

Substances

  • Blood Proteins
  • Hemoglobins
  • Oxyhemoglobins
  • Serum Albumin
  • Ethanol
  • Methemoglobin
  • Bilirubin