来自大肠杆菌的多核糖体上肽基嘌呤霉素的合成。
Peptidyl-puromycin synthesis on polyribosomes from Escherichia coli.
作者信息
Pestka S
出版信息
Proc Natl Acad Sci U S A. 1972 Mar;69(3):624-8. doi: 10.1073/pnas.69.3.624.
Abstract
Peptide bond synthesis was studied with native polyribosomes of E. coli. With the use of this system for transpeptidation, it was possible to show that a single K(+) activates the ribosome monomers of polyribosomes; that protonation of a single group (probably imidazole or an N-terminal amino group) with a pK(a) equal to about 7.2 inactivates the transpeptidase complex; that Mn(++) can substitute for Mg(++), but that Ca(++), spermidine, and putrescine do so only very poorly; and that the K(m) for puromycin in this system is about 2.4 x 10(-6) M.
摘要
利用大肠杆菌的天然多核糖体研究了肽键合成。使用该转肽系统，可以表明单个K(+)激活多核糖体的核糖体单体；单个pK(a)约为7.2的基团（可能是咪唑或N端氨基）质子化会使转肽酶复合体失活；Mn(++)可以替代Mg(++)，但Ca(++)、亚精胺和腐胺的替代效果很差；该系统中嘌呤霉素的K(m)约为2.4×10(-6)M。
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