An RNA molecule copurifies with RNase P activity from Xenopus laevis oocytes.
Utilizing a procedure for the purification of RNase P from Xenopus laevis germinal vesicle (GV) extracts, according to which the contamination by a large, cytoplasmic, cylindrical structure (1) is avoided, we demonstrate that the X.laevis enzyme, like the HeLa RNase P, is precipitated by anti-Th ant...
Zapisane w:
| Wydane w: | Nucleic Acids Res |
|---|---|
| Główni autorzy: | , , , |
| Format: | Artigo |
| Język: | Inglês |
| Wydane: |
Oxford University Press
1991
|
| Dostęp online: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC329436/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/1710353/ https://ncbi.nlm.nih.govhttps://doi.org/10.1093/nar/19.9.2315 |
| Etykiety: |
Nie ma etykietki, Dołącz pierwszą etykiete!
|