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 |
| 巻 | 153 |
| 発行部数 | 1 |
| DOI | |
| 出版物ステータス | 出版済み - 1 1 2011 |
Fingerprint
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
}
TY - JOUR
T1 - Purification and characterization of tributyltin-binding protein of tiger puffer, Takifugu rubripes
AU - Oba, Yumi
AU - Yamauchi, Akira
AU - Hashiguchi, Yasuyuki
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
PY - 2011/1/1
Y1 - 2011/1/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=78649704138&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=78649704138&partnerID=8YFLogxK
U2 - 10.1016/j.cbpc.2010.07.009
DO - 10.1016/j.cbpc.2010.07.009
M3 - Article
C2 - 20696274
AN - SCOPUS:78649704138
VL - 153
SP - 17
EP - 23
JO - Comparative Biochemistry and Physiology - C Toxicology and Pharmacology
JF - Comparative Biochemistry and Physiology - C Toxicology and Pharmacology
SN - 1532-0456
IS - 1
ER -