D-galactosamine-induced liver injury: a rat model to study the heterogeneity of the oligosaccharide chains of alpha 1-acid glycoprotein.

The effect of D-galactosamine on the structure of the glycan moiety of alpha 1-acid glycoprotein was studied throughout a nine days experiment. It was shown that: D-galactosamine led to an alteration of the Concanavalin A crossed immunoelectrophoresis pattern and to a decreased sialic acid content of alpha 1-acid glycoprotein. The undersialylation of alpha 1-acid glycoprotein was not linked to a change in the relative ratio of various Concanavalin A forms. At the end of the experiment (9 days after galactosamine injection), the Concanavalin A non-reactive forms of alpha 1-acid glycoprotein remained elevated whereas alanine transaminase activity, total protein and alpha-acid glycoprotein had returned to a control level. D-galactosamine-treated rats seem to be a suitable model for the study of the very fast cyclic modulations of the synthesis of the glycan moiety of glycoproteins.