Abstract
Highly purified extracellular superoxide dismutase was obtained from Streptococcus pyogenes strain 12714 (type 12) by adsorption of culture supernatant on phenyl-Sepharose following preparative isoelectric focusing of eluates and a final gel filtration purification on Superdex 200. The purified superoxide dismutase of S. pyogenes was found to be a homodimer. The monomeric protein had a molecular mass of 22 442 Da and an isoelectric point of 4.0. The enzymatic activity was strongly manganese-dependent. The N-terminal sequence of the purified mature protein was AIILPELPYAYDALEPQFDA and corresponded to the first amino acids following the methionine initiation codon with no evidence of a leader sequence for the mature protein. The DNA sequence of the superoxide dismutase gene of strain 12714 was found to be almost identical to the corresponding sequences reported in the gene bank data from other S. pyogenes serotypes and showed strong homology to superoxide dismutases from other Gram-positive bacteria.
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