Winkelmann D A, Kahan L
J Mol Biol. 1983 Apr 5;165(2):357-74. doi: 10.1016/s0022-2836(83)80261-7.
The reactivity of protein S4-specific antibody preparations with 30 S ribosomal subunits and intermediates of in vitro subunit reconstitution has been characterized using a quantitative antibody binding assay. Anti-S4 antibody preparations did not react with native 30 S ribosomal subunits; however, they did react with various subunit assembly intermediates that lacked proteins S5 and S12. The inclusion of proteins S5 and S12 in reconstituted particles resulted in a large decrease in anti-S4 reactivity, and it was concluded that proteins S5 and S12 are primarily responsible for the masking of S4 antigenic determinants in the 30 S subunit. The effect of S5 and S12 on S4 accessibility is consistent with data from a variety of other approaches, suggesting that these proteins form a structural and functional domain in the small ribosomal subunit.
利用定量抗体结合试验，对蛋白质S4特异性抗体制剂与30S核糖体亚基及体外亚基重构中间体的反应性进行了表征。抗S4抗体制剂不与天然30S核糖体亚基发生反应；然而，它们确实与缺乏蛋白质S5和S12的各种亚基组装中间体发生反应。在重构颗粒中加入蛋白质S5和S12会导致抗S4反应性大幅降低，得出的结论是，蛋白质S5和S12主要负责掩盖30S亚基中S4抗原决定簇。S5和S12对S4可及性的影响与来自多种其他方法的数据一致，表明这些蛋白质在小核糖体亚基中形成一个结构和功能域。
