Regulation of protein multipoint adsorption on ion-exchange adsorbent and its application to the purification of macromolecules
文献类型：期刊论文
| 作者 | Huang, Yongdong1; Bi, Jingxiu1,2; Zhao, Lan1,3; Ma, Guanghui1; Su, Zhiguo1 |
| 刊名 | PROTEIN EXPRESSION AND PURIFICATION
 |
| 出版日期 | 2010-12-01 |
| 卷号 | 74期号:2页码:257-263 |
| 关键词 | Multipoint adsorption Ligand density Steric mass-action model Bovine serum albumin Hepatitis B surface antigen Macromolecule |
| ISSN号 | 1046-5928 |
| 通讯作者 | Su, ZG |
| 英文摘要 | Ion-exchange chromatography (IEC) using commercial ionic absorbents is a widely used technique for protein purification. Protein adsorption onto ion-exchange adsorbents often involves a multipoint adsorption. In IEC of multimeric proteins or "soft" proteins, the intense multipoint binding would make the further desorption difficult, even lead to the destruction of protein structure and the loss of its biological activity. In this paper, DEAE Sepharose FF adsorbents with controllable ligand densities from 0.020 to 0.183 mmol/ml were synthesized, and then the effect of ligand density on the static ion-exchange adsorption of bovine serum albumin (BSA) onto DEAE Sepharose FF was studied by batch adsorption technique. Steric mass-action (SMA) model was employed to analyze the static adsorption behavior. The results showed that the SMA model parameters, equilibrium constant (K(a)), characteristic number of binding sites (upsilon) and steric factor (sigma), increased gradually with ligand density. Thus, it was feasible to regulate BSA multipoint adsorption by modulating the ligand density of ion-exchange adsorbent. Furthermore, IEC of hepatitis B surface antigen (HBsAg) using DEAE Sepharose FF adsorbents with different ligand densities was carried out, and the activity recovery of HBsAg was improved from 42% to 67% when the ligand density was decreased from 0.183 to 0.020 mmol/ml. Taking the activity recovery of HBsAg, the purification factor and the binding capacity into account, DEAE Sepharose FF with a ligand density of 0.041 mmol/ml was most effective for the purification of HBsAg. Such a strategy may also be beneficial for the purification of macromolecules and multimeric proteins. (C) 2010 Elsevier Inc. All rights reserved. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
| 类目[WOS] | Biochemical Research Methods ; Biochemistry & Molecular Biology ; Biotechnology & Applied Microbiology |
| 研究领域[WOS] | Biochemistry & Molecular Biology ; Biotechnology & Applied Microbiology |
| 关键词[WOS] | VIRUS SURFACE-ANTIGEN ; HYDROPHOBIC INTERACTION CHROMATOGRAPHY ; SIZE-EXCLUSION CHROMATOGRAPHY ; CHINESE-HAMSTER OVARY ; BOVINE SERUM-ALBUMIN ; MASS-ACTION MODEL ; LIGAND DENSITY ; AFFINITY-CHROMATOGRAPHY ; DISTRIBUTIONS ; EQUILIBRIUM |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000283206700018 |
| 公开日期 | 2013-11-12 |
| 版本 | 出版稿 |
| 源URL | [http://ir.ipe.ac.cn/handle/122111/5565]  |
| 专题 | 过程工程研究所_生化工程国家重点实验室 |
| 作者单位 | 1.Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, Beijing 100190, Peoples R China 2.Univ Adelaide, Sch Pharmaceut Engn, Adelaide, SA 5005, Australia 3.Chinese Acad Sci, Grad Univ, Beijing 100049, Peoples R China |
| 推荐引用方式 GB/T 7714 | Huang, Yongdong,Bi, Jingxiu,Zhao, Lan,et al. Regulation of protein multipoint adsorption on ion-exchange adsorbent and its application to the purification of macromolecules[J]. PROTEIN EXPRESSION AND PURIFICATION,2010,74(2):257-263. |
| APA | Huang, Yongdong,Bi, Jingxiu,Zhao, Lan,Ma, Guanghui,&Su, Zhiguo.(2010).Regulation of protein multipoint adsorption on ion-exchange adsorbent and its application to the purification of macromolecules.PROTEIN EXPRESSION AND PURIFICATION,74(2),257-263. |
| MLA | Huang, Yongdong,et al."Regulation of protein multipoint adsorption on ion-exchange adsorbent and its application to the purification of macromolecules".PROTEIN EXPRESSION AND PURIFICATION 74.2(2010):257-263. |
入库方式： OAI收割
来源：过程工程研究所
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