Phenprocoumon Binding to Bovine and Human α1-Acid Glycoprotein
✍ Scribed by Jason Lauritsen; Edward C. Shane
- Publisher
- Elsevier Science
- Year
- 1997
- Tongue
- English
- Weight
- 92 KB
- Volume
- 55
- Category
- Article
- ISSN
- 0026-265X
No coin nor oath required. For personal study only.
✦ Synopsis
The binding of the anticoagulant drug phenprocoumon to bovine and human a 1 -acid glycoprotein (AGP) was studied using a fluorescence titration technique. Phenprocoumon was found to have one moderate strength binding site on bovine AGP with n Å (0.78 { 0.04) and a Scatchard association constant, K Å (2.2 { 0.1) 1 10 4 M 01 . Phenprocoumon was bound more strongly to human AGP; a primary binding site was found with binding affinity, n 1 K 1 Å 4.6 1 10 5 M 01 , along with weaker secondary binding, n 2 K 2 Å 1.8 1 10 4 M 01 . ᭧ 1997 Academic Press
Methods
Racemic phenprocoumon was a gift of Hoffmann-La Roche, Inc. (Nutley, NJ). Bovine and human a 1 -AGP were obtained from the Sigma Chemical Company (St. Louis, MO). All other reagents were analytical grade. Solutions were buffered with
📜 SIMILAR VOLUMES
We investigated the binding of propranolol (PL), disopyramide (DP), and verapamil (VP) enantiomers by human alpha(1)-acid glycoprotein (AGP; also called orosomucoid) and the relationships between the extent of drug binding and lipophilicity, desialylation, and genetic variants of AGP. Desialylation
The interaction of several phenothiazine neuroleptics with alpha 1-acid glycoprotein was investigated using circular dichroism and equilibrium dialysis techniques. For chlorpromazine only, one high-affinity binding site of the protein was found. The binding of the drug to this single site generated