Andus T, Gross V, Tran-Thi T A, Heinrich P C
FEBS Lett. 1983 Jan 10;151(1):10-4. doi: 10.1016/0014-5793(83)80331-7.
The biosynthesis and secretion of alpha 2-macroglobulin was studied in rat hepatocyte primary cultures. After immunoprecipitation of alpha 2-macroglobulin from a cell homogenate and the hepatocyte medium, two forms of alpha 2-macroglobulin with app. Mr of 176000 and 182000, respectively, were identified. A precursor-product relationship for the two alpha 2-macroglobulin forms was demonstrated by a pulse-chase experiment. The cellular form of alpha 2-macroglobulin could be deglycosylated by endoglucosaminidase H, whereas the medium form of alpha 2-macroglobulin remained unaffected. On the other hand, only the medium form of alpha 2-macroglobulin was found to be susceptible to neuraminidase. In vitro translation of rat liver poly(A)+ RNA resulted in a translation product of an app. Mr of 162000.
在大鼠肝细胞原代培养物中研究了α2-巨球蛋白的生物合成与分泌。从细胞匀浆和肝细胞培养基中免疫沉淀α2-巨球蛋白后，鉴定出两种形式的α2-巨球蛋白，其表观分子量分别约为176000和182000。通过脉冲追踪实验证明了这两种α2-巨球蛋白形式存在前体-产物关系。细胞形式的α2-巨球蛋白可被内切葡糖胺酶H去糖基化，而培养基形式的α2-巨球蛋白则不受影响。另一方面，仅发现培养基形式的α2-巨球蛋白对神经氨酸酶敏感。大鼠肝脏聚腺苷酸加尾RNA的体外翻译产生了一种表观分子量约为162000的翻译产物。
