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

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11 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)17-23
Number of pages7
JournalComparative Biochemistry and Physiology - C Toxicology and Pharmacology
Issue number1
Publication statusPublished - Jan 2011

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Physiology
  • Aquatic Science
  • Animal Science and Zoology
  • Toxicology
  • Cell Biology
  • Health, Toxicology and Mutagenesis


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