Isolation of physically and enzymically homogeneous Escherichia coli elongation factor G.
作者信息
Rohrbach M S, Bodley J W
出版信息
Methods Enzymol. 1979;60:606-14. doi: 10.1016/s0076-6879(79)60057-5.
PMID:379536
Abstract
摘要
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Isolation of physically and enzymically homogeneous Escherichia coli elongation factor G.物理和酶学性质均一的大肠杆菌延伸因子G的分离
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引用本文的文献
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The ribosome-in-pieces: binding of elongation factor EF-G to oligoribonucleotides that mimic the sarcin/ricin and thiostrepton domains of 23S ribosomal RNA.破碎核糖体：延伸因子EF-G与模拟23S核糖体RNA的肌动蛋白/蓖麻毒素及硫链丝菌素结构域的寡核糖核苷酸的结合
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Carboxyl-terminal amino acid residues in elongation factor G essential for ribosome association and translocation.延伸因子G中对于核糖体结合和转位至关重要的羧基末端氨基酸残基。
J Bacteriol. 1994 Nov;176(22):7038-44. doi: 10.1128/jb.176.22.7038-7044.1994.
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