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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Bibliografiske detaljer

Udgivet i:	Nucleic Acids Res
Principais autores:	Doria, M, Carrara, G, Calandra, P, Tocchini-Valentini, G P
Format:	Artigo
Sprog:	Inglês
Udgivet:	Oxford University Press 1991
Online adgang:	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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