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
Silkworms p50 EST database