The binding of okadaic acid analogs to recombinant OABP2.1 originally isolated from the marine sponge Halichondria okadai |
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Authors: | Keiichi Konoki Tatsuya Onoda Sachie Furumochi Yuko Cho Mari Yotsu-Yamashita Takeshi Yasumoto |
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Affiliation: | 1. Graduate School of Agricultural Science, Tohoku University, 1-1 Tsutsumidori-Amamiyamachi, Aoba-ku, Sendai 981-8555, Japan;2. Tama Laboratory, Japan Food Research Laboratories, 6-11-10 Nagayama, Tama, Tokyo 206-0025, Japan |
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Abstract: | The binding between [24-3H]okadaic acid (OA) and a recombinant OA binding protein OABP2.1 was examined using various OA analog, including methyl okadaate, norokadanone, 7-deoxy OA, and 14,15-dihydro OA, 7-O-palmitoyl DTX1, to investigate the structure activity relationship. Among them, 7-O-palmitoyl DTX1, which is one of the diarrhetic shellfish poisoning (DSP) toxins identified in shellfish, displayed an IC50 for [24-3H]OA binding at 51 ± 6.3 nM (Mean ± SD). In addition, a synthetic compound, N-pyrenylmethyl okadamide, exhibited its IC50 at 10 ± 2.9 nM (Mean ± SD). These results suggested that the recombinant OABP2.1 and the N-pyrenylmethyl okadamide might be core substances in a novel assay for the DSP toxins. |
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Keywords: | Okadaic acid Dinophysistoxins Diarrhetic shellfish poisoning Okadaic acid binding protein |
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