Pintor-Toro J A, Hernández F, López-Rivas A, Palacián E
Mol Cell Biochem. 1982 Mar 5;43(1):43-7. doi: 10.1007/BF00229538.
The reversible modification of protein amino groups with dimethylmaleic anhydride, which had already been used to dissociate proteins from the 70S ribosomes of Escherichia coli (Pintor-Toro, J. A., et al. (1979) Biochemistry 18, 3219) was applied to the preparation of protein-deficient particles from the 50S subunits. Three successive cycles of treatment with dimethylmaleic anhydride, separation of dissociated proteins and regeneration of the modified amino groups produce partially inactivated ribosomal 'cores' lacking proteins L7, L11 and L12, and having very small amounts of L1, L6 and L10. Incubation of these 'cores' with the corresponding split proteins is accompanied by complete reactivation of the polypeptide synthesizing activity as compared with control 50S subunits.
已用于从大肠杆菌70S核糖体中解离蛋白质的顺丁烯二酸二甲酸酐对蛋白质氨基进行的可逆修饰（Pintor-Toro，J.A.等人，（1979年）《生物化学》18卷，3219页）被应用于从50S亚基制备缺乏蛋白质的颗粒。用顺丁烯二酸二甲酸酐进行三个连续的处理循环、分离解离的蛋白质以及修饰氨基的再生，产生了部分失活的核糖体“核心”，这些核心缺乏蛋白质L7、L11和L12，并且含有极少量的L1、L6和L10。与对照50S亚基相比，这些“核心”与相应的裂解蛋白一起温育时，多肽合成活性会完全重新激活。
