Some sulfhydryl properties and primary structure of human erythrocyte superoxide dismutase

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Abstract
Human Cu-Zn superoxide dismutase prepared by different methods shows varying properties relevant to its sulfhydryl chemistry. A cysteine residue not found in the analogous bovine enzyme appears responsible for its unusual lability. Alkylation of this cysteine results in a marked increase in stability, and this form of the protein may be readily crystallized. The primary structure of the 153 amino acid residues found in the human protein was determined, and 82% of the residues are identical with those of the bovine enzyme. Significant variation is seen in the portion of those proteins comprising residues 17-36, with eleven changes being noted.

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