Purification and identification of the type of superoxide dismutase fromGlœocapsa sp.

Superoxide dismutase purified from the photoautotrophic cyanobacteriumGlœocapsa sp. has a molar mass of 38 kDa, as estimated by gel filtration. Inhibition pattern indicated limited resistance to H₂O₂ under conditions which entirely inhibited FeSOD. The enzyme is insensitive to cyanide and is inhibited by azide. This suggested the presence of a hybrid of two isozymes, FeSOD and a minor constituent of MnSOD. Amino acid composition of the purified SOD showed structural homology to FeSOD and MnSOD apoenzymes.