Puchkova L V, Gaitskhoki V S, Monakhov N K, Timchenko L T, Neifakh S A
Mol Cell Biochem. 1981 Mar 27;35(3):159-69. doi: 10.1007/BF02357086.
Biosynthesis of ceruloplasmin was studied in wheat germ extract programmed with polysomal RNA from rat liver. Optimal potassium concentration for the total protein-synthesizing activity and for the synthesis of immunoreactive ceruloplasmin was 96 and 186 mM respectively. 7-methylguanosine 5'-monophosphate caused two-fold inhibition of the cell-free synthesis of ceruloplasmin. Immunoprecipitated ceruloplasmin that was synthesized at optimal potassium concentration was a homogeneous polypeptide of a molecular weight about 84 kD. The addition of membrane fractions from rat liver to the incubation mixture caused the conversion of the 84 kD polypeptide into 80 kD and 65 kD polypeptides that are similar to proceruloplasmins synthesized in rat liver during in vivo pulse labelling. The suggestion is made that 84 kD polypeptide is a primary product of the translation of ceruloplasmin mRNA (preproceruloplasmin).
利用来自大鼠肝脏的多聚核糖体RNA编程的小麦胚芽提取物研究了铜蓝蛋白的生物合成。总蛋白质合成活性和免疫反应性铜蓝蛋白合成的最佳钾浓度分别为96 mM和186 mM。7-甲基鸟苷5'-单磷酸对铜蓝蛋白的无细胞合成有两倍的抑制作用。在最佳钾浓度下合成的免疫沉淀铜蓝蛋白是一种分子量约为84 kD的同质多肽。向孵育混合物中添加大鼠肝脏的膜部分会导致84 kD多肽转化为80 kD和65 kD多肽，这些多肽类似于体内脉冲标记期间大鼠肝脏中合成的前铜蓝蛋白。有人提出84 kD多肽是铜蓝蛋白mRNA（前铜蓝蛋白原）翻译的初级产物。
