title: [Various enzymatic and nonenzymatic pathways of acetaldehyde transformation].
abstract: In blood acetaldehyde is bound to hemoglobin and serum albumin and interacts with low-molecular-weight components--cysteine, glutathione. The association constants for human serum albumin and human hemoglobin are about 30 M-1 and 410 M-1, respectively. The SH-groups of hemoglobin play an essential role in the interaction of protein with acetaldehyde. The reversible complexes of acetaldehyde with proteins can transform into stable adducts after long incubation with albumin, some other blood proteins but not with immunoglobulins. Acetaldehyde participates as a substrate in the reaction of acetoin formation in homogenates of different tissues. The rate of acetoin formation is about 15 +/- 3 mmol/min per 1 gram of the tissue and essentially increases in the presence of pyruvate.
authors.forename: I B
authors.initials: IB
authors.lastname: Zavodnik
authors.forename: I I
authors.initials: II
authors.lastname: Stepuro
authors.forename: Iu M
authors.initials: IuM
authors.lastname: Ostrovskiĭ
mesh_terms: D000079:Acetaldehyde / Q000097:blood / Q000378:metabolism*; D000435:Alcoholic Intoxication / Q000097:blood / Q000378:metabolism; D001798:Blood Proteins / Q000378:metabolism*; D002852:Chromatography, Ion Exchange; D000431:Ethanol / Q000097:blood / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D011485:Protein Binding
chemical_list: D001798:Blood Proteins; D000431:Ethanol; D000079:Acetaldehyde
vernacular_title: Nekotorye fermentativnye i nefermentativnye puti prevrashcheniia atsetal'degida.