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1 tics virtually identical to the transport of sulfobromophthalein.
2 odeoxycholyltaurine) and two organic anions (sulfobromophthalein and sulfolithocholyltaurine) was mea
4 port and compares this property with that of sulfobromophthalein (BSP), a preferred OATP2B1 substrate
5 hat are known to reduce uptake of bilirubin, sulfobromophthalein (BSP), and taurocholate, had any inf
6 ular ATP reduces the V(max) for transport of sulfobromophthalein by rat hepatocytes; K(m) remains una
8 e preloaded with GSH, S-methylglutathione, S-sulfobromophthalein-glutathione, S-dinitrophenyl glutath
9 acement of NaCl with choline chloride and by sulfobromophthalein-GSH, neither of which affects RcGshT
10 he presence of extracellular taurocholate or sulfobromophthalein, indicating that GSH efflux down its
11 sma disappearance of the Oatp1a1 ligand [35S]sulfobromophthalein was correspondingly delayed in knock
12 s, we demonstrated that hepatocyte uptake of sulfobromophthalein was down-regulated by extracellular
13 La cells at 37 degrees C, the uptake of [35S]sulfobromophthalein was substantial (51.6 +/- 16.5 pmol/
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