A significant improvement in a process to produce epichlorohydrin through the use of glycerin as renewable feedstock is presented. The glycerin to epichlorohydrin (GTE) process proceeds in two chemical steps. In the first step, glycerin is hydrochlorinated with hydrogen chloride gas at elevated temperature and pressure to a mixture of 1,3-DCH (1,3-dichlorohydrin, 1,3-dichloropropan-2-ol) and 2,3-DCH (2,3-dichlorohydrin, 2,3-dichloropropan-1-ol), using a carboxylic acid catalyst. In the second step, the mixture of dichlorohydrins is converted to epichlorohydrin with a base. This solventless process represents an economically and environmentally advantageous, atom-efficient process to an existing commodity chemical that can employ a renewable resource for its primary feedstock.
The binding of acetaminophen, lidocaine, phenobarbital, phenytoin, theophylline, and valproic acid to human serum alpha-1 acid glycoprotein (orosomucoid) and to human serum albumin separately in vitro was investigated using equilibrium dialysis of the unlabeled drugs. Each drug was studied at a therapeutic concentration. Alpha-1 acid glycoprotein was studied at one elevated and two physiological concentrations, whereas albumin was studied at one physiological and two low concentrations. The nonphysiological concentrations were consistent with those that might be seen in a variety of clinical conditions. Acetaminophen, phenobarbital, theophylline, and valproic acid showed negligible binding to alpha-1 acid glycoprotein. However, lidocaine and phenytoin demonstrated binding to this protein, and increases in the alpha-1 acid glycoprotein concentration produced decreases in the unbound (free) or "active" concentration of these two drugs. All drugs but acetaminophen bound to albumin, and decreases in the albumin concentration yielded increases in the unbound (free) or "active" concentration of the remaining 5 drugs. These findings are significant when lidocaine, phenytoin, phenobarbital, theophylline, or valproic acid are used in patients with clinical conditions that may affect the concentration of these two binding proteins.
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