Effects of Calcium, Magnesium, Tobramycin and Theophylline on Phenobarbitone Binding to Serum Proteins
| Autor: | J.F. Escanero, L. Rabadan, L. Pérez-Gallardo |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
medicine.medical_specialty
chemistry.chemical_element Calcium 030226 pharmacology & pharmacy Biochemistry 03 medical and health sciences 0302 clinical medicine Theophylline Internal medicine medicine Tobramycin Humans Drug Interactions Magnesium Enzyme inducer biology business.industry Biochemistry (medical) Aminoglycoside Blood Proteins Cell Biology General Medicine Blood proteins Endocrinology chemistry Phenobarbital 030220 oncology & carcinogenesis biology.protein business Protein Binding medicine.drug |
| Zdroj: | Journal of International Medical Research. 18:408-414 |
| ISSN: | 1473-2300 0300-0605 |
| Popis: | Binding of phenobarbitone to human serum proteins was determined in vitro using ultrafiltration. At therapeutic concentrations of 10–600|μM, 63.51 ± 2.5% of the phenobarbitone was bound to total serum proteins. The binding kinetics were non-saturable and the plasma apparent affinity coefficient ( NKa) was 0.791 ± 0.09 for normal serum and 0.664 ± 0.06 for chromatographed serum. Tobramycin and theophylline at therapeutic concentrations of 10 and 15 μg/ml, respectively, reduced NKa compared with the values found in normal serum. Calcium and especially magnesium at physiological concentrations of 2.5 and 5 mM, respectively, increased NKa compared with values obtained in chromatographed serum, whereas at supraphysiological concentrations of magnesium of 15 mM NKa was reduced. It is concluded that free phenobarbitone concentrations in serum can be modified by calcium, magnesium, tobramycin and theophylline, and this fact must be considered when studying enzyme induction and other properties of phenobarbitone. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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