Purification and characterization of tributyltin-binding protein of tiger puffer, Takifugu rubripes
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- 作者：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
- 关键词：Tributyltin ; Xenobiotics ; Tiger puffer ; Lipocalin ; Phylogenetic analysis
- 刊名：Comparative Biochemistry and Physiology, Part C
- 出版年：2011
- 出版时间：January 2011
- 年：2011
- 卷：153
- 期：1
- 页码：17-23
- 全文大小：826 K
文摘
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.