Cytosolic copper- and zinc-containing superoxide dismutase was purified 136-fold with an overall yield of 2.5% to apparent electrophoretic homogeneity from the dimorphic pathogenic fungus, Candida albicans. The molecular mass of the native enzyme was 39.4 kDa and the enzyme was composed of two identical subunits with a molecular mass of 19.6 kDa. The enzyme was stable in the range of pH 4.0-9.0 and up to 55 degrees C. The ultraviolet-visible absorption spectrum of the enzyme showed the absorption band of copper- and zinc-containing superoxide dismutase at 660 nm. The atomic absorption analysis revealed that the enzyme contained 0.87 g-atom of copper and 0.79 g-atom of zinc per mole of subunit. The N-terminal amino acid sequence alignments up to the 40th residue showed that copper- and zinc-containing superoxide dismutase from C. albicans has high similarity to other eukaryotic copper- and zinc-containing superoxide dismutases. The sod1 encoding copper- and zinc-containing superoxide dismutase has been cloned using a polymerase chain reaction fragment as a probe. Sequence analysis of the sod1 predicted a copper- and zinc-containing superoxide dismutase that contains 154 amino acids with a molecular mass of 16143 Da and displayed 79%, 69%, and 57% sequence identity to the homologues of Neurospora crassa, Saccharomyces cerevisiae, and bovine, respectively. The cloned sod1 contained an intron of 245 nucleotides, which was verified by reverse transcription-polymerase chain reaction.

• PMID: 10216241
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Journal Article | Research Support, Non-U.S. Gov't

Authors

Hwang CS, Rhie G, Kim ST, Kim YR, Huh WK, Baek YU, Kang SO

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