The asialoglycoprotein receptor, the hepatic binding lectin for galactose-terminated glycoproteins, has been isolated and characterized from human, rabbit and rat liver. Several recent studies have shown the existence of the same receptor in murine liver. However, the biochemical structure of the receptor in murine liver has not been resolved. In this paper, we describe the identification and purification of the receptor for asialoglycoproteins from murine liver. The purified receptor has three polypeptides with apparent molecular weights of 42,000, 45,000 and 51,000, respectively, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Furthemore, our studies suggest that the receptor from murine liver is very similar to its counterpart in rat liver, although some potential interesting differences have also been observed. Initial studies indicate that this receptor is well conserved in different mouse strains.