Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
4530078 | Aquatic Toxicology | 2011 | 6 Pages |
Abstract
Tributyltin-binding protein type 1 (TBT-bp1) is a member of the lipocalin family of proteins which bind to small hydrophobic molecules. In this study, we expressed a recombinant TBT-bp1 (rTBT-bp1, ca. 35Â kDa) in a baculovirus expression system and purified the protein from the hemolymph of silkworm larvae injected with recombinant baculovirus. After incubation of a mixture of rTBT-bp1 and TBT and its fractionation by means of gel filtration chromatography, TBT was detected in the elution peak of rTBT-bp1, confirming the binding potential of rTBT-bp1 for TBT. An assay of the ability of rTBT-bp1 or native TBT-bp1 (nTBT-bp1) to restore osteoblastic activity inhibited by TBT showed that co-treatment of the scales with rTBT-bp1 or nTBT-bp1 in combination with TBT restored osteoblastic activity in goldfish scales, whereas treatment with TBT alone significantly inhibited osteoblastic activity. These results suggest that TBT-bp1 as a lipocalin member might function to decrease the toxicity of TBT by binding to TBT.
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Authors
Hina Satone, Jae Man Lee, Yumi Oba, Takahiro Kusakabe, Eriko Akahoshi, Shizuho Miki, Nobuo Suzuki, Yuichi Sasayama, Mohamed Nassef, Yohei Shimasaki, Shun-ichiro Kawabata, Tsuneo Honjo, Yuji Oshima,