Neutral deoxyribonucleases of HeLa S3 cells: electrophoretic separation, characterization, substrate specificity and mode of action.

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  • Author(s): Slor H; Lev-Sobe T; Zöllner J
  • Source:
    European journal of biochemistry [Eur J Biochem] 1980; Vol. 108 (1), pp. 67-72.
  • Publication Type:
    Journal Article
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies Country of Publication: England NLM ID: 0107600 Publication Model: Print Cited Medium: Print ISSN: 0014-2956 (Print) Linking ISSN: 00142956 NLM ISO Abbreviation: Eur J Biochem Subsets: MEDLINE
    • Publication Information:
      Publication: -2004: Oxford, UK : Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
      Original Publication: Berlin, New York, Springer.
    • Subject Terms:
    • Abstract:
      Extracts of HeLa S3 cells were electrophoresed on polyacrylamide gels; gel slices were eluted and the eluates were assayed for DNase activities against native and denatured DNA substrates in the presence of MgCl2 or Na2EDTA. Aliquots of each eluate were also assayed for their ability to nick the circular supercoiled PM2 phage DNA to distinguish endonucleases from exonucleases. Peaks of endonuclease activities were characterized as forming 3'-phospho-oligonucleotides or 5'-phospho-oligonucleotides by the use of oligonucleotides produced by these enzymes as substrates for the 5'-phosphate-specific snake venom exonuclease. The total activity of DNases in gel eluates was much higher than that in cell extract applied to the gel, indicating the presence of inhibitors in the cell extract.
    • Accession Number:
      0 (DNA, Circular)
      0 (DNA, Single-Stranded)
      0 (DNA, Viral)
      9G34HU7RV0 (Edetic Acid)
      EC 3.1.- (Deoxyribonucleases)
      I38ZP9992A (Magnesium)
    • Publication Date:
      Date Created: 19800101 Date Completed: 19801125 Latest Revision: 20190620
    • Publication Date:
      20231215
    • Accession Number:
      10.1111/j.1432-1033.1980.tb04696.x
    • Accession Number:
      6773764