Protein adsorption to poly(ethylenimine)-modified Sepharose FF: III. Comparison between different proteins
文献类型：期刊论文
| 作者 | Hong, Yan1,2; Liu, Na1,2; Wei, Wei4; Yu, Lin-Ling1,2,3; Ma, Guanghui3; Sun, Yan1,2,3 |
| 刊名 | JOURNAL OF CHROMATOGRAPHY A
 |
| 出版日期 | 2014-05-16 |
| 卷号 | 1342期号:1页码:30-36 |
| 关键词 | Ion exchange chromatography Protein adsorption Kinetics Poly(ethylenimine) Albumin gamma-Globulin |
| ISSN号 | 0021-9673 |
| 其他题名 | J. Chromatogr. A |
| 中文摘要 | Previously, we studied bovine serum albumin (BSA) uptake to poly(ethylenimine) (PEI)-grafted Sepharose resins, and an ionic capacity (IC) range (600-740 mmol/L) for steep increases of both protein capacity (q(m)) and effective pore diffusion coefficient (D-e) was found. In this work, seven PEI-grafted. Sepharose FF resins at IC range of 270-1030 mmol/L were synthesized to investigate the effect of protein properties on the adsorption and uptake kinetics using BSA and y-globulin as two model proteins. For BSA, the change trends of qm and De values with IC were well consistent with the previous results. For 'y-globulin, the q values increased slowly till reaching a maximum value at IC= 560 mmol/L and then decreased rapidly at IC> 560 mol/L. The De values nearly kept unchanged at low ICs (IC< 460 mmol/L), and increased steeply at IC> 460 mmol/L till reaching a maximum at 680 mmol/L (De/Do = 0.48 0.01). After that increase, the De values for y-globulin dropped quickly at IC > 680 mol/L, which was not observed for BSA. It is interesting to note that in the narrodoubtw IC range of 460-680 mmol/L, the De values of -y-globulin increased dramatically for more than four folds. Moreover, it is notable that the IC range where the hopping of De values occurred for y-globulin was earlier than that for BSA (460 vs. 560 mmol/L). The earlier hopping of "y-globulin uptake rate was attributed to its larger size and less net charge, which facilitated the happenings of the "chain delivery" effect. The quick drops of both qm and De values for y-globulin at IC> 680 mmol/L were considered due to its large size, which led to the significant decrease of its effective pore volume. The results indicate that both PEI layer and protein size played important roles in protein adsorption to PEIgrafted resins, and further prove the "chain delivery" effect did contributed significantly to the uptake rate hopping in the PEI-grafted resins. This work could also help the design and selection of resins based on protein characteristics and benefit optimization of practical chromatographic processes for therapeutic proteins with PEI-grafted anion exchangers. 0 2014 Elsevier B.V. All rights reserved. |
| 英文摘要 | Previously, we studied bovine serum albumin (BSA) uptake to poly(ethylenimine) (PEI)-grafted Sepharose resins, and an ionic capacity (IC) range (600-740 mmol/L) for steep increases of both protein capacity (q(m)) and effective pore diffusion coefficient (D-e) was found. In this work, seven PEI-grafted. Sepharose FF resins at IC range of 270-1030 mmol/L were synthesized to investigate the effect of protein properties on the adsorption and uptake kinetics using BSA and y-globulin as two model proteins. For BSA, the change trends of qm and De values with IC were well consistent with the previous results. For 'y-globulin, the q values increased slowly till reaching a maximum value at IC= 560 mmol/L and then decreased rapidly at IC> 560 mol/L. The De values nearly kept unchanged at low ICs (IC< 460 mmol/L), and increased steeply at IC> 460 mmol/L till reaching a maximum at 680 mmol/L (De/Do = 0.48 0.01). After that increase, the De values for y-globulin dropped quickly at IC > 680 mol/L, which was not observed for BSA. It is interesting to note that in the narrodoubtw IC range of 460-680 mmol/L, the De values of -y-globulin increased dramatically for more than four folds. Moreover, it is notable that the IC range where the hopping of De values occurred for y-globulin was earlier than that for BSA (460 vs. 560 mmol/L). The earlier hopping of "y-globulin uptake rate was attributed to its larger size and less net charge, which facilitated the happenings of the "chain delivery" effect. The quick drops of both qm and De values for y-globulin at IC> 680 mmol/L were considered due to its large size, which led to the significant decrease of its effective pore volume. The results indicate that both PEI layer and protein size played important roles in protein adsorption to PEIgrafted resins, and further prove the "chain delivery" effect did contributed significantly to the uptake rate hopping in the PEI-grafted resins. This work could also help the design and selection of resins based on protein characteristics and benefit optimization of practical chromatographic processes for therapeutic proteins with PEI-grafted anion exchangers. 0 2014 Elsevier B.V. All rights reserved. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine ; Physical Sciences |
| 类目[WOS] | Biochemical Research Methods ; Chemistry, Analytical |
| 研究领域[WOS] | Biochemistry & Molecular Biology ; Chemistry |
| 关键词[WOS] | ION-EXCHANGE CHROMATOGRAPHY ; LASER-SCANNING MICROSCOPY ; GRAFTED AGAROSE MEDIA ; CATION-EXCHANGERS ; KINETICS ; TRANSPORT ; CAPACITY ; MECHANISM ; MATRIX ; LAYER |
| 收录类别 | SCI |
| 原文出处 | |
| 语种 | 英语 |
| WOS记录号 | WOS:000335804500005 |
| 公开日期 | 2014-08-28 |
| 版本 | 出版稿 |
| 源URL | [http://ir.ipe.ac.cn/handle/122111/10910]  |
| 专题 | 过程工程研究所_研究所（批量导入） |
| 作者单位 | 1.Tianjin Univ, Sch Chem Engn & Technol, Dept Biochem Engn, Tianjin 300072, Peoples R China 2.Tianjin Univ, Sch Chem Engn & Technol, Key Lab Syst Bioengn, Minist Educ, Tianjin 300072, Peoples R China 3.Collaborat Innovat Ctr Chem Sci & Engn Tianjin, Tianjin 300072, Peoples R China 4.Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, Beijing 100190, Peoples R China |
| 推荐引用方式 GB/T 7714 | Hong, Yan,Liu, Na,Wei, Wei,et al. Protein adsorption to poly(ethylenimine)-modified Sepharose FF: III. Comparison between different proteins[J]. JOURNAL OF CHROMATOGRAPHY A,2014,1342(1):30-36. |
| APA | Hong, Yan,Liu, Na,Wei, Wei,Yu, Lin-Ling,Ma, Guanghui,&Sun, Yan.(2014).Protein adsorption to poly(ethylenimine)-modified Sepharose FF: III. Comparison between different proteins.JOURNAL OF CHROMATOGRAPHY A,1342(1),30-36. |
| MLA | Hong, Yan,et al."Protein adsorption to poly(ethylenimine)-modified Sepharose FF: III. Comparison between different proteins".JOURNAL OF CHROMATOGRAPHY A 1342.1(2014):30-36. |
入库方式： OAI收割
来源：过程工程研究所
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