Bovine erythrocyte superoxide dismutase. Complete amino acid sequence

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

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Abstract

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
Volume249
Issue number22
Publication statusPublished - Dec 1 1974
Externally publishedYes

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ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Steinman, H. M., Naik, V. R., Abernethy, J. L., & Hill, R. L. (1974). Bovine erythrocyte superoxide dismutase. Complete amino acid sequence. Journal of Biological Chemistry, 249(22), 7326-7338.