The binding of physostigmine to human serum albumin
| Autor: | Robin Whelpton, Peter R. Hurst |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
medicine.medical_specialty
Physostigmine Serum albumin Pharmaceutical Science Internal medicine medicine Cholinesterases Humans Equilibrium dialysis Binding site Chromatography High Pressure Liquid Serum Albumin Cholinesterase Pharmacology Binding Sites Chromatography biology Chemistry Albumin Metabolism Human serum albumin Kinetics Endocrinology biology.protein medicine.drug |
| Zdroj: | Journal of Pharmacy and Pharmacology. 42:804-805 |
| ISSN: | 2042-7158 0022-3573 |
| DOI: | 10.1111/j.2042-7158.1990.tb07027.x |
| Popis: | The binding of [3H]physostigmine to crystallized human serum albumin (HSA) has been investigated using equilibrium dialysis. The percentage bound to 1% (w/v) HSA decreased from 18 to 4% as the total concentration of physostigmine increased from 3.3 nM to 2.7 μM (0.9 to 750 ng mL−1). A single class of specific binding sites with a large affinity constant, K = 8 × 107 L mol−1, was identified. The concentration of binding sites was approximately 3 nM. The Michaelis constants for human serum cholinesterase and albumin were the same; an explanation for these results is that the drug is binding to a trace cholinesterase, in the albumin. |
| Databáze: | OpenAIRE |
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