The purification of human recombinant leptin
- VernacularTitle:重组人瘦素的分离纯化
- Author:
Xianjun LIU
- Publication Type:Journal Article
- Keywords:
Human recombinant leptin;
Purifacation;
Ion exchange chromatography;
Hydrophobic interaction chromatography
- From:
Journal of Chongqing Medical University
1986;0(04):-
- CountryChina
- Language:Chinese
-
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.
