PUBLICATION

Primary structure and properties of Mn-superoxide dismutase from scallop adductor muscle

Authors
Ikebuchi, M., Takeuchi, K., Yamane, T., Ogikubo, O., Maeda, T., Kimura, H., and Ohkubo, I.
ID
ZDB-PUB-051214-5
Date
2006
Source
The international journal of biochemistry & cell biology   38(4): 521-532 (Journal)
Registered Authors
Keywords
Mn-superoxide dismutase, Purification, Characterization, Structure, Scallop adductor muscle, Amino acid sequence, cDNA sequence
MeSH Terms
  • Amino Acid Sequence
  • Animals
  • Humans
  • Molecular Sequence Data
  • Pectinidae/enzymology*
  • Pectinidae/genetics
  • Protein Structure, Tertiary
  • Sequence Analysis, Protein
  • Sequence Homology, Amino Acid
  • Superoxide Dismutase/chemistry*
  • Superoxide Dismutase/genetics
  • Superoxide Dismutase/isolation & purification
PubMed
16324874 Full text @ Int. J. Biochem. Cell Biol.
Abstract
Manganese-superoxide dismutase was purified to homogeneity from scallop adductor muscle using DEAE-Sephacel, Buthyl-Cellulofine and Superdex 200pg column chromatographies. The molecular weights of the purified enzyme were calculated to be 22,321.4 according to time-of-flight mass spectrometry, and to be approximately 95,000 and 93,000 on Superdex 200pg column chromatography and non-denatured PAGE, respectively, and were calculated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis to be 24,000 and 25,000 in the absence and 25,000 in the presence of beta-mercaptoethanol. These findings suggested that the native enzyme is composed of four identical subunits. Other properties of scallop adductor muscle manganese-superoxide dismutase, including pH stability and heat stability, were also determined. We determined the partial amino acid sequences of purified manganese-superoxide dismutase using digestions by bromocyan and lysyl endopeptidase and also determined the manganese-superoxide dismutase cDNA structure. The amino acid sequence of the enzyme obtained using both methods showed homology to those of vertebrates such as human, bovine, chicken, Xenopus and zebrafish manganese-superoxide dismutases (64.91, 65.35, 64.47, 63.27 and 64.60%, respectively). We also predicted the 3D structure of scallop adductor muscle manganese-superoxide dismutase using molecular operating environment and compared its structure with those of other manganese-superoxide dismutases. The overall structure of scallop adductor muscle manganese-superoxide dismutase was very similar to those of other species, including human and Aspergillus.
Genes / Markers
Figures
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Antibodies
Orthology
Engineered Foreign Genes
Mapping