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- Publisher
- Oxford University Press
- Copyright
- © 1986 Japanese Biochemical Society
- ISSN
- 0021-924X
- eISSN
- 1756-2651
- DOI
- 10.1093/oxfordjournals.jbchem.a135596
- Publisher site
- See Article on Publisher Site
Abstract
Abstract The complete amino acid sequence of Cu,Zn-superoxide dismutase (SOD) from spinach leaves has been determined on the basis of peptides obtained by cyanogen bromide (BrCN) cleavage and by enzymic hydrolyses with Achromobacter lyticus lysylendopeptidase, Staphylococcus aureus V8 protease, trypsin, and thermolysin. The spinach SOD consists of a total of 154 amino acid residues with alanine as the amino(N-)terminus and valine as the carboxy(C-)terminus. The present sequence, which has been established for the enzyme from a plant, is also highly homologous to those of the enzymes from other species. Especially, the residues essential for metal binding and enzyme activity have been extensively conserved among all of the Cu,Zn-SODs hitherto analyzed. This content is only available as a PDF. © 1986 Japanese Biochemical Society
Journal
The Journal of Biochemistry – Oxford University Press
Published: Apr 1, 1986