47(P-4) ヒガンフグ血漿中のサキシトキシン、テトロドトキシン結合蛋白質の精製、性状、cDNAクローニング(ポスター発表の部)

概要

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We purified a novel soluble glycoprotein that binds to saxitoxin and tetrodotoxin from plasma of the puffer fish, Fugu pardalis, and named it puffer fish saxitoxin and tetrodotoxin binding protein (PSTBP). PSTBP possessed a binding capacity of 10.6 nmol/mg protein and a K_d of 14.6 nM for ^3H-saxitoxin in equilibrium binding assays. ^3H-Saxitoxin (10 nM) binding to PSTBPs was half-inhibited by the presence of tetrodotoxin and saxitoxin at 12 μM and 8.5 nM, respectively. From the results of gel filtration chromatography (200 kDa) and SDS-PAGE (104 kDa), PSTBP was suggested to be a noncovalently linked dimer of a single subunit. PSTBP was completely deglycosylated by Glycopeptidase F producing a single band at 42 kDa. Two highly homologous cDNAs coding PSTBP (PSTBP1 and PSTBP2, the predicted amino acid identity 93%), were obtained from a cDNA library of F. pardalis liver. Presumably, PSTBP is involved in accumulation and/or excretion of the toxins in puffer fish.
天然有機化合物討論会の論文
2001-09-01