Hong W, Le A V, Doyle D
Department of Biological Sciences, State University of New York at Buffalo 14260.
Hepatology. 1988 May-Jun;8(3):553-8. doi: 10.1002/hep.1840080320.
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. Furthermore, 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.
去唾液酸糖蛋白受体是一种能与末端含半乳糖的糖蛋白结合的肝凝集素,已从人、兔和大鼠肝脏中分离出来并进行了特性分析。最近的几项研究表明,小鼠肝脏中也存在相同的受体。然而,小鼠肝脏中该受体的生化结构尚未明确。在本文中,我们描述了从小鼠肝脏中鉴定和纯化去唾液酸糖蛋白受体的过程。通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳测定,纯化后的受体有三条多肽链,其表观分子量分别为42,000、45,000和51,000。此外,我们的研究表明,小鼠肝脏中的受体与其在大鼠肝脏中的对应物非常相似,不过也观察到了一些潜在的有趣差异。初步研究表明,该受体在不同小鼠品系中高度保守。