摘要
A novel biormimetic ligand, N-benzyloxycarbonyl-L-tyrosine (N-cbZ-L-Tyr), was screened by a combination method of molecular docking and immobilized receptor technique. Then, N-cbZ-L-Tyr was immobilized on Sepharose CL-4B to prepare a specific affinity adsorbent for immunoglobulin G (IgG). Scatchard analysis of the binding isotherm for IgG on the adsorbent gave an association constant (Ka) of 4.91 × 106m-1 and a theoretical maximum adsorption capacity of 17.3 mg IgG/mL gel. IgG with a purity of 98% was separated from human plasma by this new affinity adsorbent.
| 源语言 | 英语 |
|---|---|
| 页(从-至) | 1109-1115 |
| 页数 | 7 |
| 期刊 | Biomedical Chromatography |
| 卷 | 20 |
| 期 | 10 |
| DOI | |
| 出版状态 | 已出版 - 10月 2006 |
| 已对外发布 | 是 |
指纹
探究 'Screening and chromatographic assessing of a novel lgG biomimetic ligand' 的科研主题。它们共同构成独一无二的指纹。引用此
- APA
- Author
- BIBTEX
- Harvard
- Standard
- RIS
- Vancouver