TY - JOUR
T1 - Molecular and biochemical characterization of manganese-containing superoxide dismutase from the silkworm, Bombyx mori
AU - Yamamoto, Kohji
AU - Zhang, Pingbo
AU - He, Ningjia
AU - Wang, Yongqiang
AU - Aso, Yoichi
AU - Banno, Yutaka
AU - Fujii, Hiroshi
N1 - Funding Information:
We are grateful to Dr. T. Shimada (University of Tokyo, Tokyo, Japan) and Dr. K. Mita (National Institute of Agrobiological Sciences, Tsukuba, Japan) for supplying plasmid DNA. We are also grateful to Dr. Y. Hiromasa (Kansas State University, Manhattan, KS) for critical reading of an early draft. This work is supported by the National Bio-resources project (RR2002) of the Ministry of Education, Science, and Culture of Japan.
PY - 2005/12
Y1 - 2005/12
N2 - 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°C. Its activity was never affected by incubation at pH 7 for 30 min below 50°C.
AB - 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°C. Its activity was never affected by incubation at pH 7 for 30 min below 50°C.
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U2 - 10.1016/j.cbpb.2005.09.002
DO - 10.1016/j.cbpb.2005.09.002
M3 - Article
C2 - 16236537
AN - SCOPUS:27844457093
SN - 0305-0491
VL - 142
SP - 403
EP - 409
JO - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
JF - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
IS - 4
ER -