Distinguishing between Mn-containing and Fe-containing superoxide dismutases in crude extracts of cells

Thomas Kirby, Janice Blum, Itzhak Kahane, Irwin Fridovich

Research output: Contribution to journalArticle

58 Scopus citations

Abstract

Superoxide dismutases containing manganese or iron can be resolved by exposure to low pH in the presence of guanidinium chloride. Apoenzymes so produced are inactive and are reactivated only by the metal characteristic of the native enzymes. In crude extracts of procaryotes, which may contain the iron enzymes or the manganese enzyme or both together, one can, by resolution followed by treatment with Fe(II) or Mn(II), identify and distinguish these enzymes. This method was validated with extracts of Escherichia coli, known to contain both types of enzymes, and was then used to demonstrate the presence of an iron superoxide dismutase in Alcaligenes faecalis and of manganese superoxide dismutases in Streptococcus sanguis, S. lactis, Bacillus megaterium, and Acholeplasma laidlawii. The A. laidlawii enzyme was found to have a molecular weight of ~41,000.

Original languageEnglish (US)
Pages (from-to)551-555
Number of pages5
JournalArchives of Biochemistry and Biophysics
Volume201
Issue number2
DOIs
StatePublished - May 1980
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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