Ribonucleases from porcine brain. Partial purification and properties.:Partial Purification and Properties

J-STAGE
  • NISHIKAWA Kazuya
    Department of Biophysics and Biochemistry, Faculty of Science, University of Tokyo
  • TAKAHASHI Kenji
    Department of Biophysics and Biochemistry, Faculty of Science, University of Tokyo
  • ANDO Toshio
    Department of Biophysics and Biochemistry, Faculty of Science, University of Tokyo

抄録

1. An acid ribonuclease was partially purified from an acetone powder of porcine brain. This enzyme was an acidic protein with a molecular weight of around 70, 000. It acted on yeast RNA optimally at about pH 5.9, yielding only a mixture of 3'-mononucleotides, and therefore appears to be an exonuclease. It did not hydrolyze heat-denatured calf thymus DNA or bis(p-nitrophenyl) phosphate. It was fairly unstable to heat and acid.<br> 2. An alkaline ribonuclease was partially purified from the same source simultaneously. This enzyme was a basic protein with a molecular weight of 25, 000-26, 000. It was a pyrimidine-specific endoribonuclease, and acted on yeast RNA optimally at around pH 7.4. It did not hydrolyze heat-denatured calf thymus DNA or bis(p-nitrophenyl) phosphate. It was fairly stable to heat and acid.

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