| dc.contributor.author |
Platis, D |
en |
| dc.contributor.author |
Foster, G |
en |
| dc.date.accessioned |
2014-06-06T06:45:20Z |
|
| dc.date.available |
2014-06-06T06:45:20Z |
|
| dc.date.issued |
2003 |
en |
| dc.identifier.uri |
http://dx.doi.org/10.1016/S1046-5928(03)00187-6 |
en |
| dc.identifier.uri |
http://62.217.125.90/xmlui/handle/123456789/2374 |
|
| dc.subject |
Protein Expression |
en |
| dc.subject |
Viral Infection |
en |
| dc.subject |
Biological Value |
en |
| dc.subject |
Escherichia Coli |
en |
| dc.subject |
Specific Activity |
en |
| dc.title |
High yield expression, refolding, and characterization of recombinant interferon α2/α8 hybrids in Escherichia coli |
en |
| heal.type |
journalArticle |
en |
| heal.identifier.primary |
10.1016/S1046-5928(03)00187-6 |
en |
| heal.publicationDate |
2003 |
en |
| heal.abstract |
Interferons (IFNs) are a family of pleiotropic cytokines used for the treatment of various viral infections and cancers. The low-cost production of IFNs with high biological value and the discovery of IFNs with improved properties are important for the treatment of these diseases as well as for understanding the physiological functions of these compounds. We describe a protein expression system |
en |
| heal.journalName |
Protein Expression and Purification |
en |
| dc.identifier.doi |
10.1016/S1046-5928(03)00187-6 |
en |