Fries E, Gustafsson L, Peterson P A
EMBO J. 1984 Jan;3(1):147-52. doi: 10.1002/j.1460-2075.1984.tb01775.x.
Pulse-chase experiments in conjunction with subcellular fractionation and quantitative immunoprecipitation have been used to study the intracellular transport of four secretory proteins, albumin, transferrin, prealbumin and retinol-binding protein, in isolated rat hepatocytes. The proteins were found to be transported from the endoplasmic reticulum (ER) to the Golgi complex (GC) at greatly different rates (t1/2 = 14-137 min), indicating that transport of secretory proteins between these organelles is effected by a selective, possibly receptor-mediated process and not through bulk phase transfers. The transport from the Golgi complex to the medium was rapid for all proteins (t1/2 approximately 15 min) and possibly occurred at the same rate. Consistent with these kinetic data, the amount of a rapidly transported protein (albumin) in the GC fraction was found to be high (relative to its amount in the ER fraction) whereas the amount of a slowly transported protein (transferrin) in the GC fraction was found to be low, as determined by radioimmunoassays.
结合亚细胞分级分离和定量免疫沉淀的脉冲追踪实验，已用于研究分离的大鼠肝细胞中四种分泌蛋白（白蛋白、转铁蛋白、前白蛋白和视黄醇结合蛋白）的细胞内运输。发现这些蛋白质从内质网（ER）运输到高尔基体复合体（GC）的速率差异很大（t1/2 = 14 - 137分钟），这表明这些细胞器之间分泌蛋白的运输是由一个选择性的、可能是受体介导的过程实现的，而不是通过批量转运。对于所有蛋白质来说，从高尔基体复合体到培养基的运输都很快（t1/2约为15分钟），并且可能以相同的速率发生。与这些动力学数据一致，通过放射免疫测定法测定发现，快速运输的蛋白质（白蛋白）在GC部分中的量较高（相对于其在内质网部分中的量），而缓慢运输的蛋白质（转铁蛋白）在GC部分中的量较低。
