warfarin and oxazepam-hemisuccinate

warfarin has been researched along with oxazepam-hemisuccinate* in 2 studies

Other Studies

2 other study(ies) available for warfarin and oxazepam-hemisuccinate

Article	Year
Use of a human serum albumin-based high-performance liquid chromatography chiral stationary phase for the investigation of protein binding: detection of the allosteric interaction between warfarin and benzodiazepine binding sites. Journal of pharmaceutical sciences, 1991, Volume: 80, Issue:2 The interaction between the benzodiazepine and the warfarin binding sites in human serum albumin (HSA) has been investigated using an HSA-based HPLC chiral stationary phase (HSA-CSP). (R)-Warfarin and (S)-warfarin were added to the mobile phase and racemic mixtures of oxazepam, lorazepam, and their hemisuccinic derivatives were injected onto the HSA-CSP. The presence of (R)-warfarin in the mobile phase did not significantly affect the chromatographic retention (expressed as capacity factor, k') of the investigated benzodiazepine hemisuccinate derivatives. The presence of (S)-warfarin did not significantly affect the k' of oxazepam and oxazepam hemisuccinate, but resulted in a dramatic increase in the k' of (S)-lorazepam hemisuccinate and also improved the enantiomeric resolution of lorazepam. These results confirm the existence of an allosteric interaction between the benzodiazepine binding site and the warfarin binding site. Furthermore, the study indicates that chromatography on the silica-immobilized HSA can detect interactions between binding sites on the protein. This can be of great importance in the determination of drug-drug interactions. Topics: Allosteric Regulation; Allosteric Site; Benzodiazepines; Chromatography, High Pressure Liquid; Humans; Lorazepam; Oxazepam; Protein Binding; Serum Albumin; Stereoisomerism; Warfarin	1991
The interaction of serum albumins with various drugs in aqueous solution. Gel permeation, calorimetric, and fluorescence data. Biophysical chemistry, 1979, Volume: 10, Issue:3-4 Thermodynamic data relative to the reversible interaction between human or bovine serum albumin and some organic ligands (S- and R-warfarin, d- and l-oxazepam hemisuccinate, phenyl-butazone, fluorescein) in dilute aqueous solution were determined by means of gel permeation chromatography and microcalorimetric measurements. From an analysis of these data and on the basis of fluorescence titrations the identity of the "primary" binding site on the proteins for some ligands was evidenced, while in other cases a cooperative binding of two different ligands to different binding sites could be discerned. Topics: Animals; Binding Sites; Calorimetry; Cattle; Chromatography, Gel; Fluoresceins; Humans; Kinetics; Oxazepam; Phenylbutazone; Protein Binding; Serum Albumin; Serum Albumin, Bovine; Spectrometry, Fluorescence; Warfarin	1979

Article

Year

Use of a human serum albumin-based high-performance liquid chromatography chiral stationary phase for the investigation of protein binding: detection of the allosteric interaction between warfarin and benzodiazepine binding sites.

Journal of pharmaceutical sciences, 1991, Volume: 80, Issue:2

The interaction between the benzodiazepine and the warfarin binding sites in human serum albumin (HSA) has been investigated using an HSA-based HPLC chiral stationary phase (HSA-CSP). (R)-Warfarin and (S)-warfarin were added to the mobile phase and racemic mixtures of oxazepam, lorazepam, and their hemisuccinic derivatives were injected onto the HSA-CSP. The presence of (R)-warfarin in the mobile phase did not significantly affect the chromatographic retention (expressed as capacity factor, k') of the investigated benzodiazepine hemisuccinate derivatives. The presence of (S)-warfarin did not significantly affect the k' of oxazepam and oxazepam hemisuccinate, but resulted in a dramatic increase in the k' of (S)-lorazepam hemisuccinate and also improved the enantiomeric resolution of lorazepam. These results confirm the existence of an allosteric interaction between the benzodiazepine binding site and the warfarin binding site. Furthermore, the study indicates that chromatography on the silica-immobilized HSA can detect interactions between binding sites on the protein. This can be of great importance in the determination of drug-drug interactions.

Topics: Allosteric Regulation; Allosteric Site; Benzodiazepines; Chromatography, High Pressure Liquid; Humans; Lorazepam; Oxazepam; Protein Binding; Serum Albumin; Stereoisomerism; Warfarin

1991

The interaction of serum albumins with various drugs in aqueous solution. Gel permeation, calorimetric, and fluorescence data.

Biophysical chemistry, 1979, Volume: 10, Issue:3-4

Thermodynamic data relative to the reversible interaction between human or bovine serum albumin and some organic ligands (S- and R-warfarin, d- and l-oxazepam hemisuccinate, phenyl-butazone, fluorescein) in dilute aqueous solution were determined by means of gel permeation chromatography and microcalorimetric measurements. From an analysis of these data and on the basis of fluorescence titrations the identity of the "primary" binding site on the proteins for some ligands was evidenced, while in other cases a cooperative binding of two different ligands to different binding sites could be discerned.

Topics: Animals; Binding Sites; Calorimetry; Cattle; Chromatography, Gel; Fluoresceins; Humans; Kinetics; Oxazepam; Phenylbutazone; Protein Binding; Serum Albumin; Serum Albumin, Bovine; Spectrometry, Fluorescence; Warfarin

1979