Degradation of RNA in rat reticulocytes. I. Purification and properties of rat reticulocyte RNase

Sataro Goto, Den'Ichi Mizuno

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A RNase has been partially purified from rat reticulocytes induced by phenylhydrazine. This enzyme has an optimum pH of 7.5 and degrades RNA endonucleolytically as evidenced by the analysis of degradation products. The activity is destroyed by heat treatment (pH 6.5, 80 °, 5 min). Many metal ions are inhibitory for the activity. The enzyme was inactivated almost completely by 0.5 mm HgCl2. Monovalent ions, including Nad, KCl, NH4Cl, and (NH4)2SO4, inhibit the enzyme by about 90% at concentrations of 0.1-0.2 m. The molecular weight of this enzyme is about 16,000 as determined by gel filtration. A latent RNase with higher molecular weight is present in the crude extract of the cells.

Original languageEnglish
Pages (from-to)64-70
Number of pages7
JournalArchives of Biochemistry and Biophysics
Issue number1
Publication statusPublished - Jul 1971


ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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