| Affinity Purification of Insulin by Peptide-Ligand Affinity Chromatography |
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| 作者姓名： | 董晓燕 付丽棠 俞海青 |
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| 作者单位： | School of Chemical Engineering and Technology Tianjin University，School of Chemical Engineering and Technology，Tianjin University，School of Chemical Engineering and Technology，Tianjin University，Tianjin 300072，China，Tianjin 300072，China，Tianjin 300072，China |
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| 基金项目： | 国家自然科学基金;教育部长江学者和创新团队发展计划 |
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| 摘 要： | The affinity heptapeptide(HWWWPAS)for insulin,selected from phage display library,was coupled to EAH Sepharose 4B gel and packed to a 1-mL column.The column was used for the affinity purification of insulin from protein mixture and commercial insulin preparation.It was observed that the minor impurity in the commercial insulin was removed by the affinity chromatography.Nearly 40 mg of insulin could be purified with the 1-mL affinity column.The results revealed the high specificity and capacity of the affinity column for insulin purification.Moreover,based on the analysis of the amino acids in the peptide sequence,shorter peptides were designed and synthesized for insulin chromatography.As a result,HWWPS was found to be a good alternative to HWWWPAS,while the other two peptides with three or four amino acids showed weak affinity for insulin.The results indicated that the peptide sequence of HWWWPAS was quite conservative for specific binding of insulin.
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| 关 键 词： | 亲和力 提取技术 胰岛素 缩氨酸 色谱分离法 |
| 修稿时间： | 2007-03-02 |
Affinity Purification of Insulin by Peptide-Ligand Affinity Chromatography |
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| DONG Xiaoyan,FU Litang,YU Haiqing.Affinity Purification of Insulin by Peptide-Ligand Affinity Chromatography[J].Transactions of Tianjin University,2007,13(5):313-317. |
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| Authors: | DONG Xiaoyan FU Litang YU Haiqing |
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| Institution: | School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, China |
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| Abstract: | The affinity heptapeptide(HWWWPAS)for insulin,selected from phage display library,was coupled to EAH Sepharose 4B gel and packed to a 1-mL column.The column was used for the affinity purification of insulin from protein mixture and commercial insulin preparation.It was observed that the minor impurity in the commercial insulin was removed by the affinity chromatography.Nearly 40 mg of insulin could be purified with the 1-mL affinity column.The results revealed the high specificity and capacity of the affinity column for insulin purification.Moreover,based on the analysis of the amino acids in the peptide sequence,shorter peptides were designed and synthesized for insulin chromatography.As a result,HWWPS was found to be a good alternative to HWWWPAS,while the other two peptides with three or four amino acids showed weak affinity for insulin.The results indicated that the peptide sequence of HWWWPAS was quite conservative for specific binding of insulin. |
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| Keywords: | affinity chromatography insulin purification peptide ligand ligand design |
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