The purification of human recombinant leptin / 重庆医科大学学报
Journal of Chongqing Medical University
;
(12)1986.
Article
Dans Chinois
| WPRIM
| ID: wpr-571389
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.
Texte intégral:
Disponible
Indice:
WPRIM (Pacifique occidental)
langue:
Chinois
Texte intégral:
Journal of Chongqing Medical University
Année:
1986
Type:
Article
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