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Purification and properties of a manganese-containing superoxide dismutase from acholeplasma laidlami

Hoppe-Seyler's Zeitschrift fur Physiologische Chemie, ISSN: 1437-4315, Vol: 365, Issue: 1, Page: 577-586
1984
  • 7
    Citations
  • 0
    Usage
  • 1
    Captures
  • 0
    Mentions
  • 5,874
    Social Media
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Metrics Details

  • Citations
    7
    • Citation Indexes
      7
  • Captures
    1
  • Social Media
    5,874
    • Shares, Likes & Comments
      5,874
      • Facebook
        5,874

Article Description

From the prokaryotic microorganism Acholeplasma laidlami the major manganese-containing superoxide dismutase has been purified to homogeneity, as judged by Polyacrylamide gel electrophoresis. The molecular mass of the enzyme was found to be 41 500 Da. It consists of two subunits of identical size and has an iso- electric point of 6.4. The enzyme contains 0.51 ± 0.05 atoms of manganese per subunit. Its amino-acid composition and light absorption spectra are presented and compared with Mn- and Fe-containing superoxide dismutases from other prokaryotic organisms. Copyright © by Walter de Gruyter & Co.

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