An RNA molecule copurifies with RNase P activity from Xenopus laevis oocytes.
Nucleic Acids Res
; 19(9): 2315-20, 1991 May 11.
Article
in En
| MEDLINE
| ID: mdl-1710353
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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
RNA
/
RNA, Catalytic
/
Endoribonucleases
Limits:
Animals
/
Humans
Language:
En
Journal:
Nucleic Acids Res
Year:
1991
Document type:
Article