Various enzymatic and nonenzymatic pathways of acetaldehyde transformation
Zavodnik, I.B.; Stepuro, I.I.; Ostrovskiĭ, I.M.
Ukrainskii Biokhimicheskii Zhurnal 60(4): 51-57
1988
ISSN/ISBN: 0201-8470 PMID: 3188257 Document Number: 308133
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.