Single-step purification of recombinant human interleukin-6 employing DEAE-Seph-arose weak anionic-exchange chromatography
- VernacularTitle:DEAE-Sepharose阴离子交换柱一步纯化重组人IL-6
- Author:
Xiumei DUAN
;
Yan TAN
;
Shufen XU
- Publication Type:Journal Article
- Keywords:
Interieukin-6 Purification Activity
- From:
Chinese Journal of Immunology
1999;0(12):-
- CountryChina
- Language:Chinese
-
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.
