Bovine erythrocyte superoxide dismutase. Complete amino acid sequence

H. M. Steinman, V. R. Naik, J. L. Abernethy, R. L. Hill

Research output: Contribution to journalArticlepeer-review

174 Scopus citations


The complete primary structure of reduced and S carboxymethylated bovine erythrocyte superoxide dismutase has been derived through analysis of peptides from peptic, plasmin, and hydroxylamine digests of the intact polypeptide chain, and from chymotryptic, subtilisin, and dilute acid digests of derived peptides. From these data, the unique amino acid sequence of 151 residues was deduced, corresponding to a mol wt of 15,600, in each of the 2 apparently identical subunits of the protein molecule.

Original languageEnglish (US)
Pages (from-to)7326-7338
Number of pages13
JournalJournal of Biological Chemistry
Issue number22
StatePublished - 1974
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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