TP7 Metallic and Organometallic Distribution and Effects
201 Oregon Ballroom
1:20 PM - 4:40 PM, Tuesday
() Relation between tributyltin-binding proteins and tributyltin in serum of Japanese flounder, Paralichthys olivaceus.
Oshima, Y1, Shimasaki, Y1, Tawaratsumida, Y1, Sakamoto, T2, Mitufuji, Y1, Takahashi, E1, Kitano, S3, Honjo, T1, 1 Kyushu University, Fac. of Agriculture, Fukuoka, Japan2 Trans Genic Inc, Kumamoto, Japan3 Kumamoto Univerity, Fac. of Science, Kumamoto, Japan
ABSTRACT- We reported earlier that tributyltin (TBT) accumulated in blood at concentrations 10-times higher than in liver and muscle in cultured and wild fishes; and that the TBT was bound to a specific protein in the serum of Japanese flounder, Paralichthys olivaceus (Oshima et al, 1997). We also purified and identified a TBT-binding protein (TBTBP1) from the serum of Japanese flounder. (Shimasaki et al, 2002). The amino acid sequence of TBTBP1 deduced from the cDNA sequence indicated a novel protein in the SWISS-PROT database. However, high homology was obtained with saxitoxin and tetrodotoxin binding protein isolated from swell fish, Takifugu pardalis. We also identified other type of TBT-binding protein (TBTBP2). We prepared polyclonal antibodies from synthesized C-terminal amino sequences of TBTBP1 and 2. The concentrations of TBTBPs were measured by western-blotting analysis, and the concentrations of TBT in serum were measured in Japanese flounder. High concentrations of TBT (∼266 ngTBT/ml-serum) were detected in serums of field and cultured Japanese flounder. Also, high concentrations of TBTBP1 were detected in serum of all fish, with there being no difference among samples. However, the concentrations of TBTBP2 were varied and significantly correlated with the concentration of TBT in serum. Furthermore, TBTBPs were detected in mucous on the body surface of the flounder. These results demonstrated that TBTBPs might play an important role in the kinetics of TBT in fish.
Key words: tributyltin, Japanese flounder, tributyltin-binding protein