Single-step purification of recombinant human interleukin-6 employing DEAE-Seph-arose weak anionic-exchange chromatography / 中国免疫学杂志
Chinese Journal of Immunology
;
(12)1999.
Artículo
en Chino
| WPRIM
| ID: wpr-536361
ABSTRACT
Abstract Objective:
To prepare high-purification and high-specific activity of recombinant human interleukin-6 (rhIL-6).Methods:
The rhIL-6 was obstained from inclusion body expressed by IPTG-induced pT7.7hIL-6 expressed vector using extracting,denature and refolding techniques. The rhTL-6 was further purified by anionic-exchange chromatography. Activity of rhIL-6 was measured by 3H-TdR method.Results:
After a single-step purification,the product purity reach 95% and it's specific activity was 3.0 x 10~8 U/mg.Conclusion:
This scheme of puri-fication was an easy way requiring rhTL-6.
Texto completo:
Disponible
Índice:
WPRIM (Pacífico Occidental)
Idioma:
Chino
Revista:
Chinese Journal of Immunology
Año:
1999
Tipo del documento:
Artículo
Similares
MEDLINE
...
LILACS
LIS