Abstract
Analysis of soluble peptides derived from tryptic and chymotryptic digestions of carboxymethylated human superoxide dismutase gives primary structural information for approximately 67% of the protein. Regions so far elucidated appear to be highly homologous to the corresponding bovine enzyme; in particular Cys 6 and the two cysteine residues 55 and 144, which form the intrasubunit disulfide bond of the bovine enzyme, are conserved. A cluster of three substitutions including the fourth cysteine residue unique to the human enzyme has been found in positions 107–109 and may be related to the presence of persulfide groups in the human enzyme. The single tryptophan residue of the human protein is not homologous to the single tyrosine residue of the bovine protein.
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