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The role of protein L16 and its fragments in the peptidyltransferase activity of 50-S ribosomal subunits
| Content Provider | Scilit |
|---|---|
| Author | Maimets, Tovio Ustav, Mart Villems, Richard |
| Copyright Year | 1983 |
| Description | Journal: Journal of Biological Inorganic Chemistry Two large polypeptide fragments of ribosomal protein L16 were obtained by limited hydrolysis with trypsin and chymotrypsin. The chymotryptic fragment, lacking nine N-terminal amino acids residues, is fully active in the restoration of the peptidyltransferase activity of the LiCl-stripped 50-S ribosomal subunits, whereas the tryptic fragment, lacking an additional six residues, is inactive. We also show that under the optimized ionic conditions protein L16 is not needed for the peptidyltransferase activity. |
| Related Links | http://onlinelibrary.wiley.com/doi/10.1111/j.1432-1033.1983.tb07627.x/pdf |
| Ending Page | 130 |
| Page Count | 4 |
| Starting Page | 127 |
| ISSN | 09498257 |
| e-ISSN | 14321327 |
| DOI | 10.1111/j.1432-1033.1983.tb07627.x |
| Journal | Journal of Biological Inorganic Chemistry |
| Issue Number | 1 |
| Volume Number | 135 |
| Language | English |
| Publisher | Wiley-Blackwell |
| Publisher Date | 1983-09-01 |
| Access Restriction | Open |
| Subject Keyword | Journal: Journal of Biological Inorganic Chemistry Biochemistry and Molecular Biology Analytical Chemistry Peptidyltransferase |
| Content Type | Text |
| Resource Type | Article |
| Subject | Biochemistry Inorganic Chemistry |
