Negishi K, Harada F, Nishimura S, Hayatsu H
Nucleic Acids Res. 1977 Jul;4(7):2283-92. doi: 10.1093/nar/4.7.2283.
Cytosine residues in 32P-labeled E. coli tRNA Leu 1 were modified by treatment of the tRNA with the semicarbazide-bisulfite reagents [Hayatsu, H. (1976) Biochemistry 15, 2677-2682]. Analysis of the modification sites showed that only four cytidine residues, i.e. C35, C53, C85 and C86, reacted. They were identical with the cytidines of this tRNA accessible to methoxyamine [Chang, S. E. and Ish-Horowicz, D. (1974) J. Mol. Biol. 84, 375-388] and the accessibility was consistent with the conformational features recognized for tRNA in general. The rapidity and the simple nature of this modification demonstrate that the semicarbazide-bisulfite reaction is a useful tool in studying conformations of polynucleotides.
用氨基脲 - 亚硫酸氢盐试剂处理32P标记的大肠杆菌亮氨酸tRNA1中的胞嘧啶残基[早津,H.(1976年)《生物化学》15,2677 - 2682]。对修饰位点的分析表明,只有四个胞嘧啶残基,即C35、C53、C85和C86发生了反应。它们与该tRNA中可被甲氧基胺作用的胞嘧啶相同[张,S.E.和伊什 - 霍罗维茨,D.(1974年)《分子生物学杂志》84,375 - 388],并且这种可及性与一般公认的tRNA构象特征一致。这种修饰的快速性和简单性表明,氨基脲 - 亚硫酸氢盐反应是研究多核苷酸构象的一种有用工具。