Efficient separation of homologous alpha-lactalbumin from transgenic bovine milk using optimized hydrophobic interaction chromatography
文献类型：期刊论文
| 作者 | Zhang, Yan1,2; Luo, Jian1; Bi, Jingxiu1,3; Wang, Jun1,2; Sun, Lijing1,2; Liu, Yongdong1; Zhang, Guifeng1; Ma, Guanghui1; Su, Zhiguo1 |
| 刊名 | JOURNAL OF CHROMATOGRAPHY A
 |
| 出版日期 | 2010-06-04 |
| 卷号 | 1217期号:23页码:3668-3673 |
| 关键词 | Separation Homologous protein Human alpha-lactalbumin Transgenic bovine milk |
| ISSN号 | 0021-9673 |
| 通讯作者 | Su, ZG |
| 英文摘要 | Transgenic bovine milk could be a rich source of recombinant human proteins. However, the co-presence of bovine and human homologous proteins can be a challenge for product purification. In this study, the average surface hydrophobicity and electric potential of human alpha-lactalbumin (HLA) and bovine alpha-lactalbumin (BLA) were analyzed and compared through the exposure area calculation of different amino acids. Based on the analysis, calcium independent hydrophobic interaction chromatography was selected for separation of recombinant human alpha-lactalbumin (rHLA) from BLA in transgenic bovine milk. The operating conditions for the best separation of two proteins were predicted by fluorescence data. Three commercially available HIC resins (Butyl Sepharose 4 FF, Octyl Sepharose 4 FF, Phenyl Sepharose 6 FF) were compared. The transgenic milk was skimmed and treated by pH adjustment to remove a large quantity of casein protein. The supernatant was loaded on the hydrophobic interaction chromatographic matrix. The correct elution fraction was further treated with gel filtration chromatography. The overall recovery of rHLA was up to 67.1% with the purity greater than 95%. Circular dichroism spectroscopy (CD) and mass spectrogram (MS) confirmed the native state and glycosylated form of the purified rHLA. (C) 2010 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] | PROTEINS ; ACID ; CALCIUM ; BINDING ; SITE |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000278158600005 |
| 公开日期 | 2013-11-18 |
| 版本 | 出版稿 |
| 源URL | [http://ir.ipe.ac.cn/handle/122111/6131]  |
| 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.Chinese Acad Sci, Grad Sch, Beijing 100049, Peoples R China 3.Univ Adelaide, Sch Chem Engn, Adelaide, SA 5005, Australia |
| 推荐引用方式 GB/T 7714 | Zhang, Yan,Luo, Jian,Bi, Jingxiu,et al. Efficient separation of homologous alpha-lactalbumin from transgenic bovine milk using optimized hydrophobic interaction chromatography[J]. JOURNAL OF CHROMATOGRAPHY A,2010,1217(23):3668-3673. |
| APA | Zhang, Yan.,Luo, Jian.,Bi, Jingxiu.,Wang, Jun.,Sun, Lijing.,...&Su, Zhiguo.(2010).Efficient separation of homologous alpha-lactalbumin from transgenic bovine milk using optimized hydrophobic interaction chromatography.JOURNAL OF CHROMATOGRAPHY A,1217(23),3668-3673. |
| MLA | Zhang, Yan,et al."Efficient separation of homologous alpha-lactalbumin from transgenic bovine milk using optimized hydrophobic interaction chromatography".JOURNAL OF CHROMATOGRAPHY A 1217.23(2010):3668-3673. |
入库方式： OAI收割
来源：过程工程研究所
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