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Human alpha1-acid glycoprotein (alpha1-AGP) has been used as a chiral stationary phase (CSP) for the enantioseparation of midodrine and deglymidodrine racemates in the same HPLC run. The imobilized AGP resulted as the best chiral selector for the enantioresolution of two compounds. Due to the modification of alpha1-AGP characters as a result of changing the composition of the mobile phase, an attempt study of the watery mobile phase (ionic strength and pH of the buffer, nature and concentration of the organic modifier) allowed for an increase in the enantioselectivity of the chromatographic system and an optimization of the resolution base-line of both enantiomeric pairs.

A modified Hummel-Dreyer method was used to study the binding of drugs with serum proteins by high performance capillary electrophoresis. The study was carried out to check the possible interaction between serum proteins and a highly selective beta 2-blocker, ICI 118551 (ICI). To prove the suitability of the method the protein binding of frusemide and ceftriaxone, drugs previously investigated, was also studied. The analyses were carried out by injecting a solution of s alpha(1)-acidic glycoprotein (alpha(1)-AGP) or human serum albumin in 70 mM NaH2PO4/Na2HPO4(pH 7.4) buffer into an uncoated fused silica capillary filled with the same buffer. In the capillary, maintained at a working temperature of 35 degrees C, a known amount of the ICI, frusemide or ceftriaxone was added. The method allows the bound drug to be determined directly.