Bovine erythrocyte superoxide dismutase. Complete amino acid sequence

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

Research output: Contribution to journalArticle

170 Citations (Scopus)

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
StatePublished - 1974
Externally publishedYes

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Superoxide Dismutase
Amino Acid Sequence
Erythrocytes
Amino Acids
Peptides
Subtilisin
Hydroxylamine
Fibrinolysin
Protein Subunits
Digestion
Molecules
Acids

ASJC Scopus subject areas

  • Biochemistry

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.

Bovine erythrocyte superoxide dismutase. Complete amino acid sequence. / Steinman, Howard M.; Naik, V. R.; Abernethy, J. L.; Hill, R. L.

In: Journal of Biological Chemistry, Vol. 249, No. 22, 1974, p. 7326-7338.

Research output: Contribution to journalArticle

Steinman, HM, Naik, VR, Abernethy, JL & Hill, RL 1974, 'Bovine erythrocyte superoxide dismutase. Complete amino acid sequence', Journal of Biological Chemistry, vol. 249, no. 22, pp. 7326-7338.
Steinman, Howard M. ; Naik, V. R. ; Abernethy, J. L. ; Hill, R. L. / Bovine erythrocyte superoxide dismutase. Complete amino acid sequence. In: Journal of Biological Chemistry. 1974 ; Vol. 249, No. 22. pp. 7326-7338.
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