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. 1991 May 11;19(9):2315-20.
doi: 10.1093/nar/19.9.2315.

An RNA molecule copurifies with RNase P activity from Xenopus laevis oocytes

M Doria  1 , G Carrara, P Calandra, G P Tocchini-Valentini
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Free PMC article

An RNA molecule copurifies with RNase P activity from Xenopus laevis oocytes

M Doria et al. Nucleic Acids Res. .
Free PMC article

Abstract

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 antibodies and an RNA molecule (XL RNA), 320 nucleotides long, copurifies with the activity. The sequence of XL RNA is 60% homologous to HeLa H1 RNA, therefore the two molecules seem related.

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