Purification and characterization of tributyltin-binding protein of tiger puffer, Takifugu rubripes

Yumi Oba, Akira Yamauchi, Yasuyuki Hashiguchi, Hina Satone, Shizuho Miki, Mohamed Nassef, Yohei Shimasaki, Takeshi Kitano, Miki Nakao, Shun Ichiro Kawabata, Tsuneo Honjo, Yuji Oshima

研究成果: ジャーナルへの寄稿記事

8 引用 (Scopus)

抄録

We successfully purified Trub.TBT-bpα, a tributyltin (TBT) binding protein (bp) of the tiger puffer, Takifugu rubripes. Tiger puffer was injected intraperitoneally with TBT (1.0 mg/kg body weight) and Trub.TBT-bpα was purified from serum by ammonium sulfate fractionation, gel filtration chromatography and polyacrylamide gel electrophoresis. Gel electrophoresis revealed that the Trub.TBT-bpα has a molecular mass of approximately 48.5 kDa and contains at least 40% N-glycan. The deduced 212 amino acid sequence of the protein showed the highest identity (41%, 212 amino acid overlap and E-value: 9e-42) with TBT-binding protein type 1 (TBT-bp1) of Paralichthys olivaceus (Japanese flounder). Analysis of the gene structure of Trub.TBT-bpα suggests that this protein belongs to the lipocalin superfamily, which may be important in the accumulation and elimination of TBT. Phylogenetic analysis suggests that functionalization of TBT-bps has occurred during evolution, and that the functions of this group of proteins might be important for fish survival.

元の言語英語
ページ(範囲)17-23
ページ数7
ジャーナルComparative Biochemistry and Physiology - C Toxicology and Pharmacology
153
発行部数1
DOI
出版物ステータス出版済み - 1 1 2011

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Takifugu
Tetraodontiformes
Purification
Carrier Proteins
Electrophoresis
Gels
Lipocalins
Flounder
tributyltin
Amino Acids
Proteins
Ammonium Sulfate
Molecular mass
Fractionation
Chromatography
Fish
Gel Chromatography
Polysaccharides
Polyacrylamide Gel Electrophoresis
Amino Acid Sequence

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Physiology
  • Toxicology
  • Cell Biology
  • Health, Toxicology and Mutagenesis

これを引用

Purification and characterization of tributyltin-binding protein of tiger puffer, Takifugu rubripes. / Oba, Yumi; Yamauchi, Akira; Hashiguchi, Yasuyuki; Satone, Hina; Miki, Shizuho; Nassef, Mohamed; Shimasaki, Yohei; Kitano, Takeshi; Nakao, Miki; Kawabata, Shun Ichiro; Honjo, Tsuneo; Oshima, Yuji.

:: Comparative Biochemistry and Physiology - C Toxicology and Pharmacology, 巻 153, 番号 1, 01.01.2011, p. 17-23.

研究成果: ジャーナルへの寄稿記事

Oba, Yumi ; Yamauchi, Akira ; Hashiguchi, Yasuyuki ; Satone, Hina ; Miki, Shizuho ; Nassef, Mohamed ; Shimasaki, Yohei ; Kitano, Takeshi ; Nakao, Miki ; Kawabata, Shun Ichiro ; Honjo, Tsuneo ; Oshima, Yuji. / Purification and characterization of tributyltin-binding protein of tiger puffer, Takifugu rubripes. :: Comparative Biochemistry and Physiology - C Toxicology and Pharmacology. 2011 ; 巻 153, 番号 1. pp. 17-23.
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abstract = "We successfully purified Trub.TBT-bpα, a tributyltin (TBT) binding protein (bp) of the tiger puffer, Takifugu rubripes. Tiger puffer was injected intraperitoneally with TBT (1.0 mg/kg body weight) and Trub.TBT-bpα was purified from serum by ammonium sulfate fractionation, gel filtration chromatography and polyacrylamide gel electrophoresis. Gel electrophoresis revealed that the Trub.TBT-bpα has a molecular mass of approximately 48.5 kDa and contains at least 40{\%} N-glycan. The deduced 212 amino acid sequence of the protein showed the highest identity (41{\%}, 212 amino acid overlap and E-value: 9e-42) with TBT-binding protein type 1 (TBT-bp1) of Paralichthys olivaceus (Japanese flounder). Analysis of the gene structure of Trub.TBT-bpα suggests that this protein belongs to the lipocalin superfamily, which may be important in the accumulation and elimination of TBT. Phylogenetic analysis suggests that functionalization of TBT-bps has occurred during evolution, and that the functions of this group of proteins might be important for fish survival.",
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AU - Satone, Hina

AU - Miki, Shizuho

AU - Nassef, Mohamed

AU - Shimasaki, Yohei

AU - Kitano, Takeshi

AU - Nakao, Miki

AU - Kawabata, Shun Ichiro

AU - Honjo, Tsuneo

AU - Oshima, Yuji

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