Rodewald R
J Cell Biol. 1976 Nov;71(2):666-9. doi: 10.1083/jcb.71.2.666.
Rat and rabbit IgG immunoglobulins conjugated to horseradiah peroxidase as a histochemical marker bind at 0 degrees C to the luminal surface of absorptive cells in isolated segments of jejunum from 10-12-day old rats. Binding is observed at pH 6.0, near the normal luminal pH of the duodenum and jejunum at this age, but not at pH 7.4. Furthermore, no binding occurs when cells are exposed at pH 6.0 to either free peroxidase or peroxidase conjugated to chicken or sheep IgG immunoglobulins or bovine serum albumin. The sensitivity of binding to pH suggests a means whereby immunoglobulins which are selectively absorbed by the cells can be released efficiently at the abluminal surface.
与辣根过氧化物酶结合作为组织化学标记物的大鼠和兔IgG免疫球蛋白,在0℃时结合于10 - 12日龄大鼠空肠分离段吸收细胞的腔面。在pH 6.0时可观察到结合,此pH接近该年龄十二指肠和空肠的正常腔内pH,但在pH 7.4时未观察到结合。此外,当细胞在pH 6.0下暴露于游离过氧化物酶、与鸡或羊IgG免疫球蛋白或牛血清白蛋白结合的过氧化物酶时,均未发生结合。结合对pH的敏感性提示了一种机制,通过该机制被细胞选择性吸收的免疫球蛋白可在腔外表面有效释放。