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
N1 - Funding Information:
This study was supported by a grant from the Ministry of Education, Culture, Sports, Science, and Technology of Japan ( 20580221 ).
PY - 2011/1
Y1 - 2011/1
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.
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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 -