The separation of hemoglobin-acetaldehyde adducts by cation exchange chromatography: a brief history.

Screening for alcohol abuse in its early phase, and the diagnosis of alcohol-related organ damage by laboratory tests in clinical settings, have often been unreliable. Protein-acetaldehyde adducts may be helpful in trying to solve this problem and hemoglobin, with its acetaldehyde adducts, appears to be a suitable model for studying protein-acetaldehyde adducts as condensation products of acetaldehyde, a harmful metabolite of ethanol. The modification by acetaldehyde alters the chromatographic properties of the hemoglobin molecule, producing a modified form that can be separated from other hemoglobin forms by cation exchange chromatographic techniques. The methods for the separation of hemoglobin acetaldehyde adducts have been improved in recent years, allowing us today to detect in vitro changes in hemoglobin caused by "physiological" concentrations of acetaldehyde and raising the possibility of developing a method suitable for clinical detection of hemoglobin acetaldehyde adducts.