Interaction of ethanol with blood proteins.
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.
Institute of Biochemistry, Byelorussian SSR Academy of Sciences, Grodno, USSR.
Ostrovsky YuM
I I
II
Stepuro
A N
AN
Artsukevich
I B
IB
Zavodnik
N V
NV
Konovalova
E A
EA
Lapshina
D001663:Bilirubin / Q000378:metabolism; D001798:Blood Proteins / Q000378:metabolism*; D000431:Ethanol / Q000493:pharmacokinetics* / Q000494:pharmacology; D006454:Hemoglobins / Q000378:metabolism; D006801:Humans; D008706:Methemoglobin / Q000378:metabolism; D010108:Oxyhemoglobins / Q000378:metabolism; D011487:Protein Conformation / Q000187:drug effects; D012709:Serum Albumin / Q000378:metabolism
D001798:Blood Proteins; D006454:Hemoglobins; D010108:Oxyhemoglobins; D012709:Serum Albumin; D000431:Ethanol; D008706:Methemoglobin; D001663:Bilirubin