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PMID:23291011
| Citation |
Huang, Q, Li, Q, Chen, AS and Kang, C (2013) West Nile virus protease activity in detergent solutions and application for affinity tag removal. Anal. Biochem. 435:44-6 |
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| Abstract |
Affinity tags are typically used to facilitate membrane protein purification. A protease needs to remain active in the presence of detergent to remove a fusion tag from a recombinant membrane protein. Our results show that the West Nile virus (WNV) protease activity was not affected while in the presence of a wide range of detergents. In a detergent solution, the WNV protease can remove the fusion tag from a recombinant protein containing KCNE3 and a WNV protease site. Therefore, the WNV protease may be useful as an alternative enzyme to remove affinity tags in protein purifications. |
| Links |
PubMed Online version:10.1016/j.ab.2012.12.015 |
| Keywords |
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| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
|
enables |
GO:0008233: peptidase activity |
ECO:0000314: direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
| GO:0008233: peptidase activity |
ECO:0000314: |
F |
As seen in Figure 1, WNV protease retained activity in most of the detergents tested in this study. WNV protease possesses catalytic activity in the presence of some detergents, making it useful for the removal of an affinity tag in a membrane protein preparation. It is suggested that WNV protease can be used for the preparation of a membrane protein or a transmembrane domain segment from a multi-span transmembrane protein. |
complete | ||||
See also
References
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