The Nucleases from <I>Acrocylindrium</I> sp.:II. Crystallization and Chemical Properties of Endonuclease

J-STAGE
  • SUHARA Ikuo
    Microbiological Research Laboratories, Central Research Division, Takeda Chemical Industries, Ltd.
  • YONEDA Masahiko
    Microbiological Research Laboratories, Central Research Division, Takeda Chemical Industries, Ltd.

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Description

1. The endonuclease from Acrocylindriu purified about 60-fold by means of CM-cellulose and hydroxyapatite column chromatography. This enzyme preparation was free from exonuclease, ribonuclease [ribonucleate guaninenucleotido-2'-transferase (cyclizing), EC 2. 7. 7. 26, or ribonucleate nucleotido-2'-transferase (cyclizing), EC 2. 7. 7. 17], phosphodiesterase [orthophosphoric diester phosphohydrolase, EC 3. 1. 4. 1], phosphomonoesterase [orthophosphoric monoester phosphohydrolase, EC 3. 1.3. 1 or 3. 1. 3. 2], and protease.<BR>2. Furthermore, the endonuclease was obtained as needle crystals. The crystalline endonuclease showed a single peak with the sedimentation constant of 2.5 S in an ultracentrifuge.<BR>3. The molecular weight of the crystalline endonuclease was estimated to be 19, 000-21, 000.<BR>4. It was demonstrated by amino acid analysis that the tryptophan content in the endonuclease was higher than that in Staphylococcal nuclease (1).<BR>5. The N-terminal amino acid of the enzyme was determined as asparagine or aspartic acid.<BR>6. The isoelectric point of the enzyme was pH 6.8.

Journal

  • J Biochem (Tokyo)

    J Biochem (Tokyo) 73 (3), 647-654, 1973

    The Japanese Biochemical Society

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