Factors influencing the protein binding of a new phosphodiesterase V inhibitor, DA-8159, using an equilibrium dialysis technique
| Autor: | Eun Lee, Myung Gull Lee, So H. Kim, Soon Hui Kim, Won B. Kim, Moohi Yoo, Hyun J. Shim, Jong W. Kwon |
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| Rok vydání: | 2000 |
| Předmět: |
Phosphodiesterase Inhibitors
Serum albumin Pharmaceutical Science Plasma protein binding Buffers chemistry.chemical_compound Blood plasma medicine Animals Humans Pharmacology (medical) Equilibrium dialysis Incubation Chromatography High Pressure Liquid Serum Albumin Pharmacology Sulfonamides Chromatography Molecular Structure biology Heparin Chemistry Temperature General Medicine Hydrogen-Ion Concentration Human serum albumin Pyrimidines Dextran Enzyme inhibitor biology.protein Dialysis Protein Binding medicine.drug |
| Zdroj: | Biopharmaceutics & Drug Disposition. 21:285-291 |
| ISSN: | 1099-081X 0142-2782 |
| DOI: | 10.1002/bdd.238 |
| Popis: | Various factors influencing the protein binding of DA-8159 to 4% human serum albumin (HSA) were evaluated using an equilibrium dialysis technique at an initial DA-8159 concentration of 5 µg/mL. It took approximately 8 h incubation to reach an equilibrium between 4% HSA and an isotonic phosphate buffer of pH 7.4 containing 3% of dextran (‘the buffer’) using a Spectra/Por 2 membrane (mol. wt. cut-off: 12 000–14 000) in a water bath shaker kept at 37°C and at a rate of 50 oscillations per min. The extent of binding was dependent on DA-8159 concentrations, HSA concentrations, incubation temperature, buffer pH, and alpha-1-acid glycoprotein (AAG) concentrations. The binding of DA-8159 in heparinized human plasma (93.9%) was significantly higher than in rats (81.4%), rabbits (80.4%), and dogs (82.2%), and this could be due to differences in AAG concentrations in plasma. Copyright © 2000 John Wiley & Sons, Ltd. |
| Databáze: | OpenAIRE |
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