| Autor: |
Karp, Warren B., Kinsley, Michael, Subramanyam, S. B., Robertson, Alex F. |
| Zdroj: |
Alcoholism: Clinical & Experimental Research; 1985, Vol. 9 Issue 5, p429-432, 4p |
| Abstrakt: |
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 [34C]monoacetyidiaminodiphenyl sulfone (MADDS), a deputy ligand for bilirubin, or [34C]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. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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