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| 重组人瘦素的分离纯化 | |
| 引用本文： | 刘先俊,刘方欣,漆洪波. 重组人瘦素的分离纯化[J]. 重庆医科大学学报, 2003, 28(4): 451-453,476 |
| 作者姓名： | 刘先俊 刘方欣 漆洪波 |
| 作者单位： | 1. 重庆医科大学基础医学院生化教研室,重庆,400016 2. 重庆医科大学基础医学院核医学教研室,重庆,400016 3. 重庆医科大学临床学院妇产科,重庆,400016 |
| 摘 要： | 目的：探索毕赤酵母表达的人瘦素的非亲和层析纯化方法。方法：采用强阴离子交换柱(Sepharose Qfast flow)和疏水层析柱(Phenyl Sepharose 6 fast flow)在pH7．5的条件下进行纯化。结果：经Q柱一步纯化后，产物纯度由42．3％到达89．6％，随后通过疏水层析纯化后，产物纯度达到96．2％。经SDS—PAGE证实为单一蛋白条带。结论：通过上述手段已成功分离纯化得到纯度较高的由毕赤酵母表达的重组人瘦素。 |
| 关 键 词： | 重组人瘦素 分离 纯化 疏水层析 强阴离子交换柱 |
| 文章编号： | 0253-3626(2003)04-0451-03 |
The purification of human recombinant leptin |
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| LIU Xianjun,et al. The purification of human recombinant leptin[J]. Journal of Chongqing Medical University, 2003, 28(4): 451-453,476 | |
| Authors: | LIU Xianjun et al |
| Abstract: | Objective:To explore the purification method of non- affinity chromatography for leptin expressed in Pichia Pastoris.Methods:Ion exchange chromatography (Sepharose Q fast flow) and hydrophobic interaction chromatography (Phenyl Sepharose 6 fast flow ) were used to purify human leptin in pH 7.5. Results: After purification by Q column,the purity of leptin increased from 42.3% to 89.6%.Subsequently, after hydrophobic interaction chromatography ,its purity reached 96.2%. In SDS-PAGE, leptin was shown as one specific band.Conclusion:The human recombinant leptin expressed by Pichia Pastoris yeast can be successfully purified by ion exchange chromatography plus hydrophobic interaction chromatography. |
| Keywords: | Human recombinant leptin Purifacation Ion exchange chromatography Hydrophobic interaction chromatography |
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