Drug Binding Analysis of Human α1-Acid Glycoprotein Using Capillary Electrophoresis
✍ Scribed by Yukihiro Kuroda; Akimasa Shibukawa; Terumichi Nakagawa
- Publisher
- John Wiley and Sons
- Year
- 2003
- Weight
- 72 KB
- Volume
- 34
- Category
- Article
- ISSN
- 0931-7597
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
The function of sialic acid groups at the terminal of sugar chains of human ␣ 1 -acid glycoprotein (AGP) was investigated with respect to chiral discrimination between optical isomers of basic drugs, using high-performance capillary electrophoresis/frontal analysis (HPCE/FA), a novel analytical meth
We investigated the binding of propranolol (PL), disopyramide (DP), and verapamil (VP) enantiomers by human alpha(1)-acid glycoprotein (AGP; also called orosomucoid) and the relationships between the extent of drug binding and lipophilicity, desialylation, and genetic variants of AGP. Desialylation
## Abstract Interactions between α~1~‐acid glycoprotein (AGP) and 52 basic drugs were quantified by means of highperformance liquid chromatography (HPLC). The HPLC retention parameters were related quantitatively to the hydrophobicity and molecular modelling parameters, giving rise to the predictio
## Binding studies of porphyrins to human serum albumin using affinity capillary electrophoresis The present work demonstrates that affinity capillary electrophoresis (ACE) can be employed as a valuable and powerful tool for studying the interactions between porphyrins and proteins in biological a