Binding properties of glycosylated albumin and acetaldehyde albumin.
Glucose and acetaldehyde react covalently with albumin to form the post-translationally modified group of proteins, the glycosylated albumins and the acetaldehyde albumins, respectively. This study contrasts the binding ability of a major acetaldehyde albumin fraction synthesized in vitro with glycosylated albumin. A microdialysis rate method, using either [14C]monoacetyldiaminodiphenyl sulfone (MADDS), a deputy ligand for bilirubin, or [14C]diazepam, was employed to evaluate binding at these two sites. Our results indicate that prolonged exposure of purified human serum albumin to acetaldehyde results in a major acetaldehyde albumin fraction that lacks the ability to bind MADDS and diazepam. This fraction migrates identically to albumin on SDS polyacrylamide gel electrophoresis, but exhibits microheterogeneity with a more acidic pI band as seen on analytical isoelectric focusing. We suggest that altered drug binding in alcoholics may be partially explained by altered binding ability of acetaldehyde albumins.
D000079:Acetaldehyde / Q000378:metabolism*; D000418:Albumins / Q000378:metabolism*; D000437:Alcoholism / Q000097:blood; D001663:Bilirubin / Q000378:metabolism; D003622:Dapsone / Q000031:analogs & derivatives / Q000378:metabolism; D003975:Diazepam / Q000378:metabolism; D017127:Glycation End Products, Advanced; D006801:Humans; D011485:Protein Binding; D012709:Serum Albumin / Q000378:metabolism*; D000093423:Glycated Serum Albumin
D000418:Albumins; D017127:Glycation End Products, Advanced; D012709:Serum Albumin; D003622:Dapsone; C018965:monoacetyldapsone; D000079:Acetaldehyde; D003975:Diazepam; D001663:Bilirubin; D000093423:Glycated Serum Albumin