Influence of pH on aggregation and protein binding of barbituric acid and amylobarbitone
| Autor: | W. Mikikits, D. C. Watts, R. G. Spector, Annette Skinner |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 1971 |
| Předmět: |
Polymers
Plasma protein binding Degree of polymerization Medicinal chemistry chemistry.chemical_compound Freezing Organic chemistry Bovine serum albumin Pharmacology chemistry.chemical_classification Aqueous solution Barbituric acid biology Water Serum Albumin Bovine Polymer Hydrogen-Ion Concentration Solutions Monomer chemistry Polymerization Barbiturates biology.protein Drug Mechanisms Amobarbital Dialysis Protein Binding |
| Popis: | Summary 1 Cryoscopic methods indicated that barbituric acid exists in aqueous solution as a monomer. Amylobarbitone is a monomer at pH 8, but appears to be polymerized at pH 2. The size of the oligomers increases with drug concentration. 2 Using a non-equilibrium dialysis technique supportive evidence for the monomeric form of barbituric acid and the polymerization of amylobarbitone was obtained. The degree of polymerization appeared to increase with fall in pH. Binding constants for these barbiturates with bovine serum albumin were derived, but in acid media no binding was observed. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|