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Plasma protein binding interactions hepatic clearance

Warfarin enantiomers are extensively metabolized by liver, possess a low hepatic extraction ratio, and are extensively bound (> 99%) to plasma proteins (Table 3). Therefore any change in the protein binding of warfarin enantiomers may alter the clearance and plasma concentrations of R- and S-warfarin [54]. Yacobi and Levy [54] studied the plasma protein binding of racemic and individual enantiomers of warfarin in human blood. The free fraction of R-warfarin was significantly (32%) larger than that of S-warfarin (Table 3). The authors concluded that the difference in the potency of warfarin enantiomers could not be solely explained by the observed differences in the protein binding of the individual enantiomers but rather by the intrinsic ability of R- and S-warfarin for interactions with extravascular receptors. [Pg.221]


See other pages where Plasma protein binding interactions hepatic clearance is mentioned: [Pg.111]    [Pg.74]    [Pg.101]    [Pg.320]    [Pg.327]    [Pg.24]    [Pg.213]    [Pg.471]    [Pg.175]   


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