Kiss A L, Röhlich P
2nd Department of Anatomy, Histology and Embryology, Semmelweis University of Medicine, Budapest/Hungary.
Cell Biol Int Rep. 1988 Apr;12(4):289-98. doi: 10.1016/0309-1651(88)90073-2.
Peroxidase-antiperoxidase (PAP) binding sites on the rat peritoneal macrophage surface were damaged by pronase digestion and the reappearance of functionally intact receptors was investigated morphologically and spectrophotometrically. Pronase digestion decreased the PAP binding ability of macrophages to about 40% of the original value. Removing the pronase the regeneration of ligand binding was very protracted with only about 60% intact receptors even after 30 min. From these findings we conclude that the recycling of internalized Fc receptors greatly contribute to the replenishment of receptors on the cell surface.
链霉蛋白酶消化可损伤大鼠腹膜巨噬细胞表面的过氧化物酶-抗过氧化物酶（PAP）结合位点，通过形态学和分光光度法研究功能完整受体的重新出现。链霉蛋白酶消化使巨噬细胞的PAP结合能力降至原值的约40%。去除链霉蛋白酶后，配体结合的再生过程非常缓慢，即使在30分钟后也只有约60%的完整受体。从这些发现中我们得出结论，内化Fc受体的再循环对细胞表面受体的补充有很大贡献。
