Krentler C, Pohlmann R, Hasilik A, von Figura K
Biol Chem Hoppe Seyler. 1986 Feb;367(2):141-5. doi: 10.1515/bchm3.1986.367.1.141.
Lysosomal membrane proteins and soluble lysosomal material were isolated from pulse-chase labelled human skin fibroblasts and examined for incorporation of radioactivity and affinity to immobilized mannose-6-phosphate-specific receptors. Incorporation of radioactivity into lysosomal membrane proteins was delayed by about 2 h on average when compared to that of soluble lysosomal proteins. The lack of binding indicates that a mannose-6-phosphate-independent mechanism is responsible for targeting of lysosomal membrane proteins to lysosomes. In contrast to soluble lysosomal proteins, the membrane proteins did not bind to mannose-6-phosphate specific receptors. The delayed appearance of membrane proteins in lysosomes as compared to that of soluble lysosomal proteins suggested that different pathways are utilized by the two classes of lysosomal proteins.
从脉冲追踪标记的人皮肤成纤维细胞中分离出溶酶体膜蛋白和可溶性溶酶体物质，并检测其放射性掺入情况以及与固定化的甘露糖-6-磷酸特异性受体的亲和力。与可溶性溶酶体蛋白相比，溶酶体膜蛋白的放射性掺入平均延迟约2小时。缺乏结合表明，一种不依赖甘露糖-6-磷酸的机制负责将溶酶体膜蛋白靶向溶酶体。与可溶性溶酶体蛋白不同，膜蛋白不与甘露糖-6-磷酸特异性受体结合。与可溶性溶酶体蛋白相比，溶酶体中膜蛋白出现延迟，这表明两类溶酶体蛋白利用了不同的途径。
