Ahn T I, Jeon K W
Exp Cell Res. 1985 Sep;160(1):54-62. doi: 10.1016/0014-4827(85)90235-6.
The fate of a membrane protein of the amoeba plasmalemma was studied by means of 125I iodination by lactoperoxidase, gel electrophoresis, radioautography and gamma counting. There was only one iodinatable polypeptide group with a molecular weight (MW) of 175 000 on the external surface of the plasmalemma. Two hours or more after induced phagocytosis, isolated phagolysosomal membranes contained two other smaller polypeptides with MWs of 70 000 and 35 000, respectively, suggesting that the 175 000 polypeptide was broken down to these smaller components during endocytosis. After 22 h of induced phagocytosis, isolated plasmalemma contained a 35 000 polypeptide group in addition to the 175 000 polypeptide species. The results suggested that some of the iodinatable membrane proteins were altered and recycled during endo- and exocytosis in amoebae, while others were recycled intact.
通过乳过氧化物酶介导的¹²⁵I碘化、凝胶电泳、放射自显影和γ计数等方法，研究了变形虫质膜中一种膜蛋白的命运。质膜外表面只有一个可碘化的多肽组，其分子量（MW）为175000。诱导吞噬后两小时或更长时间，分离的吞噬溶酶体膜含有另外两种较小的多肽，分子量分别为70000和35000，这表明175000的多肽在胞吞过程中被分解为这些较小的成分。诱导吞噬22小时后，分离的质膜除了含有175000的多肽种类外，还含有一个35000的多肽组。结果表明，一些可碘化的膜蛋白在变形虫的内吞和外排过程中发生了改变并被循环利用，而另一些则完整地被循环利用。
