| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2020969 | Protein Expression and Purification | 2009 | 7 Pages |
Abstract
The folding and biological activity of the purified proteins were analyzed by circular dichroism (CD) spectroscopy and flow cytometry, respectively, and compared to solubly produced CHIPS31-113 and wild-type CHIPS1-121. We show that the CHIPS variants produced in inclusion bodies can be refolded and purified to achieve equal biological activity as solubly produced CHIPS31-113 and wild-type CHIPS1-121. The truncation causes minor structural changes while purification from inclusion bodies or the soluble fraction does not further affect the structure.
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Authors
Erika Gustafsson, Cecilia Forsberg, Karin Haraldsson, Stina Lindman, Lill Ljung, Christina Furebring,