Delipidation of α1-acid glycoprotein
| Autor: | Jean-Paul Giroud, Laurence Chauvelot-Moachon, C. Durlach-Misteli, F. Tallet |
|---|---|
| Rok vydání: | 1988 |
| Předmět: |
Pharmacology
chemistry.chemical_classification Gel electrophoresis Chromatography Ethanol biology Linoleic acid Orosomucoid Plasma protein binding female genital diseases and pregnancy complications chemistry.chemical_compound chemistry Concanavalin A polycyclic compounds biology.protein Binding site Glycoprotein |
| Zdroj: | Journal of Pharmacological Methods. 20:15-28 |
| ISSN: | 0160-5402 |
| DOI: | 10.1016/0160-5402(88)90012-5 |
| Popis: | Propranolol binding to human α1-acid glycoprotein (AAG) delipidated by two methods is described. Commercial AAG (99% pure) was either precipitated by ethanol-acetone and then washed by ether, or it was precipitated by ethanol. Binding capacity was quantified by the product n × Ka where n denotes the number of binding sites and Ka the association constant (M −1 ). Propranolol binding to nondelipidated AAG ( n × Ka = 0.113 ± 0.013 μ M −1 ) was clearly increased after precipitation by ethanol-acetone ( n × Ka = 0.386 ± 0.109 μ M −1 ) or precipitation by ethanol ( n × Ka = 0.312 ± 0.096 μ M −1 ). Binding capacity potentiation cannot be due to modification of AAG microheterogeneity forms, as two-dimensional gel electrophoresis pattern of AAG in presence of concanavalin A was not altered after both methods. Recombination of precipitated AAGs with supernatant dry residue resulted in the abrogation of observed potentiation. Moreover, addition of a polar lipid, linoleic acid, (from 30 to 300 μM) strongly inhibited propranolol binding. These results indicated that glycoprotein precipitation by ethanol provided a simple method to further study binding inhibitors associated with isolated AAG. |
| Databáze: | OpenAIRE |
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