期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1973
卷号：70
期号：7
页码：1931-1935
DOI：10.1073/pnas.70.7.1931
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Cores were prepared from 50S ribosomal subunits by incubation with 0.4 M LiCl/Mg++ (0.4c cores); 0.8c cores and corresponding SP0.4-0.8 split proteins were obtained from 0.4c cores. In the fragment reaction 0.4c cores were active, but 0.8c cores were not. Activity of the 0.8c cores could be restored by reconstitution with the SP0.4-0.8 fraction. The split proteins were separated by DEAE-cellulose chromatography and Sephadex gel filtration. The peptidyltransferase activity is correlated with the amount of protein L11 added to the 0.8c core under reconstitution conditions. Whether protein L11 displays the enzymatic activity itself or is part of the enzymatic center is discussed.
