Abstract
The complete amino acid sequence of manganese superoxide dismutase isolated from Saccharomyces cerevisiae has been determined by automated Edman degradation. Peptides for sequence analysis were produced by cleavage with cyanogen bromide, hydroxylamine and S. aureus protease V8. The native enzyme consists of four identical polypeptide chains 203 residues long each containing a single sulfhydryl group and no disulfide bridges. A subunit molecular weight of 22,690 was calculated from the complete sequence. The sequence exhibits a significant degree of homology with the managanese superoxide dismutase from E. coli and B. stearothermophilus.
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Abbreviations
- ANS:
-
2-amino-1,5-naphthalene disulfonic acid
- CNBr:
-
cyanogen bromide
- GuHC1:
-
guanidinium hydrochloride
- HFBA:
-
heptafluorobutyric acid
- PMSF:
-
phenylmethylsulfonylfluoride
- Polybrene:
-
1,5-dimethyl-1,5-diazaundecamethylene polymethobromide
- PTH:
-
phenylthiohydantoin
- SOD:
-
superoxide dismutase
- THEED:
-
N,N,N′,N′-tetrakis(2-hydroxyethyl)ethylene diamine
- Tris:
-
2-amino-2-hydroxymethyl-1,3-propanediol
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Ditlow, C., Johansen, J.T., Martin, B.M. et al. The complete amino acid sequence of manganese-superoxide dismutase from Saccharomyces cerevisiae. Carlsberg Res. Commun. 47, 81–91 (1982). https://doi.org/10.1007/BF02907799
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DOI: https://doi.org/10.1007/BF02907799