枯草芽孢杆菌中的转位作用：通过肽基-[3H]嘌呤霉素合成对延伸因子G进行表征。
Translocation in Bacillus subtilis: characterization of elongation factor G by peptidyl-[3H]puromycin synthesis.
作者信息
Aharonowitz Y, Ron E Z
出版信息
J Bacteriol. 1976 Mar;125(3):1074-9. doi: 10.1128/jb.125.3.1074-1079.1976.
Abstract
This communication describes the characterization of elongation factor G from Bacillus subtilis by the translocation of "native" peptide donors. Translocation was followed by elongation factor G-dependent increase in the synthesis of peptidyl-[3H]puromycin using "washed" ribosomes carrying in vivo-bound peptidyl-transfer ribonucleic acid ("native" peptidyl-transfer ribonucleic acid) molecules as peptide donors. Such ribosomes were obtained from cell extracts by washing at a high salt concentration. The use of "native" peptide donors facilitated the study of translocation under conditions that are closer to the in vivo state than those in the methods previously employed.
摘要
本通讯描述了通过“天然”肽供体的转位对枯草芽孢杆菌延伸因子G的特性研究。转位过程通过使用携带体内结合的肽基转移核糖核酸（“天然”肽基转移核糖核酸）分子作为肽供体的“洗涤”核糖体，在延伸因子G的作用下，肽基-[3H]嘌呤霉素的合成增加来跟踪。这种核糖体是通过在高盐浓度下洗涤从细胞提取物中获得的。与先前使用的方法相比，使用“天然”肽供体有助于在更接近体内状态的条件下研究转位。
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