On-column Refolding of EC-SOD Inclusion Bodies, Purification and Stability Study / 微生物学通报
Microbiology
;
(12)1992.
Article
in Chinese
| WPRIM
| ID: wpr-684758
ABSTRACT
EC-SOD inclusion bodies was refolded on column using metal (Ni) affinity chromatography, based on the metal-binding property of His-tag. The effect of protein amount, urea removal speed and temperature on refolding was observed. We compared the different efficiency purified with Ni-sepharose and Heprain-sepharose affinity chromatography, and studied the stability of the refolded proteins. The results indicate that the inclusion bodies can be renatured with Ni-sepharose affinity chromatography. The increase of the protein amount and urea removal rate , the lower of the renaturation efficiency. Higher temperature was benefit to protein renaturation. Both the Ni-sepharose and Heprain-sepharose affinity column can be used to purified the refolded proteins, but purified by Heprain-sepharose affinity column the protein had higher activity. The activity of renatured protein was stable in 10 ℃~50℃,when pH10 its stability was lower significantly. In denaturating solution the stability of renatured protein was low.
Full text:
Available
Index:
WPRIM (Western Pacific)
Language:
Chinese
Journal:
Microbiology
Year:
1992
Type:
Article
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