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...
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| Published in: | Nucleic Acids Res |
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| Main Authors: | , , , |
| Format: | Artigo |
| Language: | Inglês |
| Published: |
Oxford University Press
1991
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| Online Access: | 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 |
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