Bovine erythrocyte superoxide dismutase. Isolation and characterization of tryptic, cyanogen bromide, and maleylated tryptic peptides

H. J. Evans, Howard M. Steinman, R. L. Hill

Research output: Contribution to journalArticle

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Abstract

Tryptic and cyanogen bromide peptides were isolated from reduced and S-carboxymethylated bovine erythrocyte superoxide dismutase, and maleylated tryptic peptides were isolated from the individual cyanogen bromide fragments. Based upon end group analyses of the intact protein and the yields and partial sequence analyses of these peptides, a partial sequence of the enzyme was deduced. From these data it was concluded that the 2 subunits of bovine dismutase appear to be chemically identical. Each subunit is acetylated at the NH2 terminus, has lysine at the COOH terminus, and contains no tryptophan.

Original languageEnglish (US)
Pages (from-to)7315-7325
Number of pages11
JournalJournal of Biological Chemistry
Volume249
Issue number22
StatePublished - 1974
Externally publishedYes

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Cyanogen Bromide
Superoxide Dismutase
Erythrocytes
Peptides
Protein Sequence Analysis
Tryptophan
Lysine
Enzymes
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

Bovine erythrocyte superoxide dismutase. Isolation and characterization of tryptic, cyanogen bromide, and maleylated tryptic peptides. / Evans, H. J.; Steinman, Howard M.; Hill, R. L.

In: Journal of Biological Chemistry, Vol. 249, No. 22, 1974, p. 7315-7325.

Research output: Contribution to journalArticle

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