Hanski C, Reutter W, Evans W H
Eur J Cell Biol. 1984 Jan;33(1):123-6.
The turnover of a mouse liver plasma membrane glycoprotein (Mr 105 k) has been studied by means of immunoprecipitation and radioactive labeling. The method of immunoprecipitation proved to be a fast and efficient way of isolating a single protein for measurement of its specific radioactivity. The half-life of the carbohydrate moiety determined using 3H-galactose was 41 h and using 3H-mannose was 23 h, whereas that of the protein moiety determined using 3H-leucine was 63 h. The implications of this differential degradation of the protein and carbohydrate moieties are discussed in terms of the recycling of glycoproteins between the plasma membrane and intracellular membranes.
通过免疫沉淀和放射性标记的方法,对小鼠肝细胞膜糖蛋白(分子量105k)的周转情况进行了研究。免疫沉淀法被证明是一种快速有效的分离单一蛋白质以测量其比放射性的方法。使用3H-半乳糖测定的碳水化合物部分的半衰期为41小时,使用3H-甘露糖测定的为23小时,而使用3H-亮氨酸测定的蛋白质部分的半衰期为63小时。根据糖蛋白在质膜和内膜之间的循环,讨论了蛋白质和碳水化合物部分这种差异降解的意义。