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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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| Autores principales: | , , , |
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| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
1991
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| Acceso en línea: | https://ncbi.nlm.nih.gov/pmc/articles/PMC329436/ https://ncbi.nlm.nih.gov/pubmed/1710353 |
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