将不同长度和氨基酸特异性的蛋白质亲和标记试剂连接到大肠杆菌甲硫氨酰-tRNAf上。
Attachment of protein affinity-labeling reagents of variable length and amino acid specificity to E. coli tRNAfMet.
作者信息
Schulman L H, Pelka H, Reines S A
出版信息
Nucleic Acids Res. 1981 Mar 11;9(5):1203-17. doi: 10.1093/nar/9.5.1203.
Abstract
Transamination with bifunctional amines in the presence of bisulfite has been used to attach side chains of variable length to the N4-position of single stranded cytidine residues in E. coli tRNAfMet. Such side chains, terminating in reactive primary amino groups, have been coupled to a variety of N-hydroxysuccinimide esters. The resulting modified tRNAs carry protein affinity labeling groups capable of covalent reaction with a variety of amino acids.
摘要
在亚硫酸氢盐存在的情况下，利用双功能胺进行转氨作用，已将可变长度的侧链连接到大肠杆菌甲酰甲硫氨酸转运核糖核酸（tRNAfMet）单链胞苷残基的N4位上。这种以反应性伯氨基结尾的侧链，已与多种N-羟基琥珀酰亚胺酯偶联。所得的修饰转运核糖核酸（tRNAs）带有能够与多种氨基酸发生共价反应的蛋白质亲和标记基团。
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