Bystrova N K, Belen'kiĭ D M
Biokhimiia. 1985 Jun;50(6):992-7.
The receptor for asialoglycoproteins was isolated from murine liver and was purified by means of biospecific chromatography on sepharose-Asialo-orosomucoid. The obtained receptor with an absorption maximum at 277 nm binds to the nonreducing terminal galactosyl residues of glycoproteins similar to the receptors from liver of other mammalians. The interaction between this receptor and desialylated glycoproteins requires the presence of calcium. The dependence of specific binding on the concentration of [125I]acialo-orosomucoid used as a ligand gives a saturating curve. The dissociation constant for the receptor-ligand complex is 0.4 X 10(-9) M. Similar to asialo-orosomucoid, the receptor binds the p-aminophenyl-beta-D-galactopyranoside derivatives of bovine serum albumin, ovalbumin and acid alpha-glucosidase synthesized by us earlier. Possible use of the asialoglycoprotein receptor as a highly specific carrier transporting the modified acid alpha-glucosidase to hepatocyte lysosomes is discussed.
脱唾液酸糖蛋白受体是从小鼠肝脏中分离出来的，并通过在琼脂糖-去唾液酸血清类黏蛋白上进行生物特异性层析进行纯化。所获得的在277nm处有最大吸收峰的受体，与糖蛋白的非还原末端半乳糖基残基结合，这与其他哺乳动物肝脏中的受体类似。该受体与去唾液酸化糖蛋白之间的相互作用需要钙的存在。特异性结合对用作配体的[125I]去唾液酸血清类黏蛋白浓度的依赖性呈现出一条饱和曲线。受体-配体复合物的解离常数为0.4×10(-9)M。与去唾液酸血清类黏蛋白相似，该受体能结合我们之前合成的牛血清白蛋白、卵清蛋白和酸性α-葡萄糖苷酶的对氨基苯基-β-D-吡喃半乳糖苷衍生物。文中讨论了脱唾液酸糖蛋白受体作为一种将修饰后的酸性α-葡萄糖苷酶转运至肝细胞溶酶体的高度特异性载体的可能用途。
