Structural analysis of peptide-acetaldehyde adducts by mass spectrometry and production of antibodies directed against nonreduced protein-acetaldehyde adducts.

@article{Lin1995StructuralAO,
  title={Structural analysis of peptide-acetaldehyde adducts by mass spectrometry and production of antibodies directed against nonreduced protein-acetaldehyde adducts.},
  author={Renee C. Lin and J. J. B. Smith and Daniela Radtke and Lawrence Lumeng},
  journal={Alcoholism, clinical and experimental research},
  year={1995},
  volume={19 2},
  pages={314-9}
}
Acetaldehyde can form protein-acetaldehyde adducts (AAs) in vivo and may play a role in the genesis of alcoholic liver disease. The nature of the chemical modification of proteins by acetaldehyde in vivo has not been elucidated. In vitro, acetaldehyde can form reversible adducts including a Schiff's base with lysine (K) and imidazolidinone with terminal amino groups of proteins such as human hemoglobin (Hb). In this study, we used FAB/MS to analyze the products of peptide-AAs (pep-AAs) formed… CONTINUE READING