Gaitskhoki V S, L'vov V M, Puchkova L V, Schwartzman A L, Neifakh S A
Mol Cell Biochem. 1981 Mar 27;35(3):171-82. doi: 10.1007/BF02357087.
Highly purified ceruloplasmin mRNA was isolated from rat liver polyribosomes. The molecular weight of ceruloplasmin mRNA is in a range from 1.05 to 1.25 . 10(6) daltons which is large enough to code for a putative precursor of ceruloplasmin (approximately 700 amino acid acids). Ceruloplasmin mRNA contains 3'-terminal poly(A) the length of which varies from 38 to 165 nucleotides. The 5'-end of ceruloplasmin mRNA is blocked with confronting m7G residue which is a component of cap I (m7G5'ppp5'XmpAp). The addition of ceruloplasmin mRNA to wheat-germ cell free system programmed the synthesis of a product that was largely precipitated by anti-ceruloplasmin immunoglobulins. The translation product was homogeneous in polyacrylamide gel-sodium dodecylsulfate electrophoresis. Cell-free translation of ceruloplasmin mRNA was sensitive to inhibition by cap analogue.
从大鼠肝脏多核糖体中分离出高度纯化的铜蓝蛋白信使核糖核酸。铜蓝蛋白信使核糖核酸的分子量在1.05至1.25×10⁶道尔顿范围内,这足以编码铜蓝蛋白的假定前体(约700个氨基酸)。铜蓝蛋白信使核糖核酸含有3'-末端多聚腺苷酸,其长度在38至165个核苷酸之间变化。铜蓝蛋白信使核糖核酸的5'-末端被与帽I(m⁷G5'ppp5'XmpAp)成分相对的m⁷G残基封闭。将铜蓝蛋白信使核糖核酸添加到无细胞小麦胚芽系统中可促使合成一种主要被抗铜蓝蛋白免疫球蛋白沉淀的产物。该翻译产物在聚丙烯酰胺凝胶-十二烷基硫酸钠电泳中是均一的。铜蓝蛋白信使核糖核酸的无细胞翻译对帽类似物的抑制敏感。