RRC ID |
575
|
Author |
Yamamoto K, Zhang P, He N, Wang Y, Aso Y, Banno Y, Fujii H.
|
Title |
Molecular and biochemical characterization of manganese-containing superoxide dismutase from the silkworm, Bombyx mori.
|
Journal |
Comp Biochem Physiol B Biochem Mol Biol
|
Abstract |
Superoxide dismutase (SOD) is responsible for the removal of superoxide anion from living organisms. In this study, cDNA encoding the manganese-containing SOD (MnSOD) from the silkworm, Bombyx mori, was isolated by reverse transcriptase-polymerase chain reaction and sequenced. The deduced amino acid sequence of the MnSOD revealed 62% identity to that of the Drosophila melanogaster; both were close to each other in a phylogenetic tree. The MnSOD was overproduced in Escherichia coli and purified. The internal structure of the recombinant MnSOD was confirmed by peptide mass fingerprinting method. The recombinant MnSOD facilitating the reduction reaction of superoxide anion retained 75% of its original activity after incubation at pH 4-11 for 24 h at 4 degrees C. Its activity was never affected by incubation at pH 7 for 30 min below 50 degrees C.
|
Volume |
142(4)
|
Pages |
403-9
|
Published |
2005-12-1
|
DOI |
10.1016/j.cbpb.2005.09.002
|
PII |
S1096-4959(05)00208-3
|
PMID |
16236537
|
MeSH |
Amino Acid Sequence
Animals
Bombyx / enzymology*
Bombyx / genetics
Bombyx / metabolism
Cloning, Molecular
DNA, Complementary / genetics
DNA, Complementary / metabolism
Hydrogen-Ion Concentration
Molecular Sequence Data
Organ Specificity
Peptide Mapping
Phylogeny
RNA Precursors / metabolism
Sequence Alignment
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Superoxide Dismutase / chemistry*
Superoxide Dismutase / genetics
Superoxide Dismutase / isolation & purification
Temperature
|
IF |
2.219
|
Times Cited |
15
|
WOS Category
|
ZOOLOGY
BIOCHEMISTRY & MOLECULAR BIOLOGY
|
Resource |
Silkworms |
p50
EST database |