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Partial purification and characterization of a double-stranded RNA-specific nuclease from human placenta.

Abstract
A double-stranded RNA-specific nuclease (ds RNase) has been isolated and partially purified from human placenta by DEAE-cellulose and DNA-cellulose column chromatography. Denatured DNA-cellulose retained most of the single-stranded RNA-specific nuclease (ss RNase) activity, whereas the ds RNase came out in the void volume. N-ethylmaleimide at a concentration of 5 mM, selectively inhibited ds RNase activity by 60% under the conditions in which the ss RNase activity was inhibited to an extent of 7%. The ds RNase was specifically inhibited by Penicillium chrysogenum viral ds RNA and by ethidium bromide. The partially purified ds RNase showed requirements for Mg+ whereas Mn2+ and NH4+ ions were inhibitory. The DEAE-enzyme cleaved 32P-labelled 45S ribosomal precursor RNAs from Yoshida ascites sarcoma cells into species that had similar electrophoretic mobilities as the mature rRNAs.
AuthorsS Kalyanaraman, A Maran, G Shanmugam
JournalMolecular biology reports (Mol Biol Rep) Vol. 9 Issue 3 Pg. 179-83 (Aug 1983) ISSN: 0301-4851 [Print] Netherlands
PMID6633520 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Ammonia
  • 2'-5'-oligo(A)-dependent endonuclease
  • Endoribonucleases
  • Magnesium
Topics
  • Ammonia (metabolism)
  • Endoribonucleases (isolation & purification, metabolism)
  • Female
  • Humans
  • Magnesium (metabolism)
  • Placenta (enzymology)
  • Pregnancy

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