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The purification of human recombinant leptin / 重庆医科大学学报
Journal of Chongqing Medical University ; (12)1986.
Artículo en Chino | 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.

Texto completo: Disponible Índice: WPRIM (Pacífico Occidental) Idioma: Chino Revista: Journal of Chongqing Medical University Año: 1986 Tipo del documento: Artículo

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Texto completo: Disponible Índice: WPRIM (Pacífico Occidental) Idioma: Chino Revista: Journal of Chongqing Medical University Año: 1986 Tipo del documento: Artículo