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.
Citation
Ikebuchi, M., Takeuchi, K., Yamane, T., Ogikubo, O., Maeda, T., Kimura, H., and Ohkubo, I. (2006) Primary structure and properties of Mn-superoxide dismutase from scallop adductor muscle. The international journal of biochemistry & cell biology. 38(4):521-532.
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
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping