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The protein itself, a 66.5-kDa protein secreted by the liver, appears to have two major xenobiotic binding sites, a large flexible site that preferentially binds dicarboxylic acids and/or bulky heterocyclic molecules with a negative charge localized in the middle of the molecule and a second smaller, more narrow, and less flexible site that preferentially binds aromatic carboxylic acids with a negative charge localized at one end away from a hydrophobic center

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