Characterization of superoxide dismutase from the fall webworm, Hyphantria cunea: Comparison of its properties to superoxide dismutase from the silkworm Bombyx mori

Kohji Yamamoto, Makoto Kimura, Yoichi Aso, Yutaka Banno, Katsumi Koga

研究成果: ジャーナルへの寄稿記事

1 引用 (Scopus)

抄録

Superoxide dismutase (SOD) is a regulatory enzyme involved in the degradation of superoxide anions in living organisms. In this study, we examined SOD from the fall webworm, Hyphantria cunea (hcSOD). A cDNA encoding hcSOD was cloned by reverse transcriptase-polymerase chain reaction. The deduced amino acid sequence of hcSOD revealed that six of seven highly conserved residues forming the Cu/Zn-binding sites were present. The hcSOD mRNA and the enzyme activity were distributed in larval tissues including fat body, midgut and hemocyte of H. cunea. A recombinant hcSOD (rhcSOD) functionally overexpressed in Escherichia coli in a soluble form that was purified to homogeneity. It was stable at pHs between 5 and 11. Incubation for 30 min at temperatures below 50°C scarcely affected the activity. All these properties, as well as CD spectra, of hcSOD or rhcSOD were highly similar to those of the Bombyx mori counterparts except for the number of Cu/Zn-binding sites and the specific activity dismutating superoxide anion to peroxide and oxygen.

元の言語英語
ページ(範囲)465-472
ページ数8
ジャーナルApplied Entomology and Zoology
42
発行部数3
DOI
出版物ステータス出版済み - 12 12 2007

Fingerprint

Hyphantria cunea
Bombyx mori
silkworms
superoxide dismutase
superoxide anion
binding sites
fat body
hemocytes
peroxides
midgut
amino acid sequences
reverse transcriptase polymerase chain reaction
enzyme activity
Escherichia coli
oxygen
degradation
organisms
enzymes
temperature

All Science Journal Classification (ASJC) codes

  • Insect Science

これを引用

@article{3b94770bdf6c48b3a6e1f9aa5f5db8a2,
title = "Characterization of superoxide dismutase from the fall webworm, Hyphantria cunea: Comparison of its properties to superoxide dismutase from the silkworm Bombyx mori",
abstract = "Superoxide dismutase (SOD) is a regulatory enzyme involved in the degradation of superoxide anions in living organisms. In this study, we examined SOD from the fall webworm, Hyphantria cunea (hcSOD). A cDNA encoding hcSOD was cloned by reverse transcriptase-polymerase chain reaction. The deduced amino acid sequence of hcSOD revealed that six of seven highly conserved residues forming the Cu/Zn-binding sites were present. The hcSOD mRNA and the enzyme activity were distributed in larval tissues including fat body, midgut and hemocyte of H. cunea. A recombinant hcSOD (rhcSOD) functionally overexpressed in Escherichia coli in a soluble form that was purified to homogeneity. It was stable at pHs between 5 and 11. Incubation for 30 min at temperatures below 50°C scarcely affected the activity. All these properties, as well as CD spectra, of hcSOD or rhcSOD were highly similar to those of the Bombyx mori counterparts except for the number of Cu/Zn-binding sites and the specific activity dismutating superoxide anion to peroxide and oxygen.",
author = "Kohji Yamamoto and Makoto Kimura and Yoichi Aso and Yutaka Banno and Katsumi Koga",
year = "2007",
month = "12",
day = "12",
doi = "10.1303/aez.2007.465",
language = "English",
volume = "42",
pages = "465--472",
journal = "Applied Entomology and Zoology",
issn = "0003-6862",
publisher = "Japanese Society of Applied Entomology and Zoology",
number = "3",

}

TY - JOUR

T1 - Characterization of superoxide dismutase from the fall webworm, Hyphantria cunea

T2 - Comparison of its properties to superoxide dismutase from the silkworm Bombyx mori

AU - Yamamoto, Kohji

AU - Kimura, Makoto

AU - Aso, Yoichi

AU - Banno, Yutaka

AU - Koga, Katsumi

PY - 2007/12/12

Y1 - 2007/12/12

N2 - Superoxide dismutase (SOD) is a regulatory enzyme involved in the degradation of superoxide anions in living organisms. In this study, we examined SOD from the fall webworm, Hyphantria cunea (hcSOD). A cDNA encoding hcSOD was cloned by reverse transcriptase-polymerase chain reaction. The deduced amino acid sequence of hcSOD revealed that six of seven highly conserved residues forming the Cu/Zn-binding sites were present. The hcSOD mRNA and the enzyme activity were distributed in larval tissues including fat body, midgut and hemocyte of H. cunea. A recombinant hcSOD (rhcSOD) functionally overexpressed in Escherichia coli in a soluble form that was purified to homogeneity. It was stable at pHs between 5 and 11. Incubation for 30 min at temperatures below 50°C scarcely affected the activity. All these properties, as well as CD spectra, of hcSOD or rhcSOD were highly similar to those of the Bombyx mori counterparts except for the number of Cu/Zn-binding sites and the specific activity dismutating superoxide anion to peroxide and oxygen.

AB - Superoxide dismutase (SOD) is a regulatory enzyme involved in the degradation of superoxide anions in living organisms. In this study, we examined SOD from the fall webworm, Hyphantria cunea (hcSOD). A cDNA encoding hcSOD was cloned by reverse transcriptase-polymerase chain reaction. The deduced amino acid sequence of hcSOD revealed that six of seven highly conserved residues forming the Cu/Zn-binding sites were present. The hcSOD mRNA and the enzyme activity were distributed in larval tissues including fat body, midgut and hemocyte of H. cunea. A recombinant hcSOD (rhcSOD) functionally overexpressed in Escherichia coli in a soluble form that was purified to homogeneity. It was stable at pHs between 5 and 11. Incubation for 30 min at temperatures below 50°C scarcely affected the activity. All these properties, as well as CD spectra, of hcSOD or rhcSOD were highly similar to those of the Bombyx mori counterparts except for the number of Cu/Zn-binding sites and the specific activity dismutating superoxide anion to peroxide and oxygen.

UR - http://www.scopus.com/inward/record.url?scp=36849060709&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=36849060709&partnerID=8YFLogxK

U2 - 10.1303/aez.2007.465

DO - 10.1303/aez.2007.465

M3 - Article

AN - SCOPUS:36849060709

VL - 42

SP - 465

EP - 472

JO - Applied Entomology and Zoology

JF - Applied Entomology and Zoology

SN - 0003-6862

IS - 3

ER -