An RNA molecule copurifies with RNase P activity fromXenopus laevisoocytes | Zendy

Margherita Doria | Zendy; G. Carrara | Zendy; Patrizia Calandra | Zendy; Glauco P. TocchiniValentini | Zendy

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An RNA molecule copurifies with RNase P activity fromXenopus laevisoocytes

Author(s) -

Margherita Doria,

G. Carrara,

Patrizia Calandra,

Glauco P. TocchiniValentini

Publication year - 1991

Publication title -

nucleic acids research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 9.008

H-Index - 537

eISSN - 1362-4954

pISSN - 0305-1048

DOI - 10.1093/nar/19.9.2315

Subject(s) - xenopus , biology , rnase p , rna , microbiology and biotechnology , computational biology , genetics , gene

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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