dc.creator | Targovnik, Alexandra Marisa | |
dc.creator | Villaverde, Marcela Solange | |
dc.creator | Arregui, Mariana Bernadett | |
dc.creator | Fogar, Mariela A. | |
dc.creator | Taboga, Oscar Alberto | |
dc.creator | Glikin, Gerardo Claudio | |
dc.creator | Finocchiaro, Liliana Maria Elena | |
dc.creator | Cascone, Osvaldo | |
dc.creator | Miranda, Maria Victoria | |
dc.date.accessioned | 2017-05-23T17:56:35Z | |
dc.date.accessioned | 2018-11-06T11:57:29Z | |
dc.date.available | 2017-05-23T17:56:35Z | |
dc.date.available | 2018-11-06T11:57:29Z | |
dc.date.created | 2017-05-23T17:56:35Z | |
dc.date.issued | 2014-03 | |
dc.identifier | Targovnik, Alexandra Marisa; Villaverde, Marcela Solange; Arregui, Mariana Bernadett; Fogar, Mariela A.; Taboga, Oscar Alberto; et al.; Expression and purification of recombinant feline interferon in the baculovirus-insect larvae system; Elsevier; Process Biochemistry; 49; 6; 3-2014; 917-926 | |
dc.identifier | 1359-5113 | |
dc.identifier | http://hdl.handle.net/11336/16878 | |
dc.identifier | 1873-3298 | |
dc.identifier.uri | http://repositorioslatinoamericanos.uchile.cl/handle/2250/1861503 | |
dc.description.abstract | Feline interferons (FeIFNs) are cytokines with antiviral, antitumor and immunomodulatory functions used as therapeutic agents in a variety of veterinary diseases. In this work, FeIFN-α7 and FeIFN-α7xArg containing eight residues of arginine were expressed in Sf9 cells and insect larvae. At 4 days post-infection (dpi), the concentrations of FeIFN-α7 and FeIFN-α7xArg in suspension culture were (1.28 ± 0.15) × 106 U ml−1 and (1.3 ± 0.2) × 106 U ml−1 respectively. The maximum expression levels of FeIFN-α7 and FeIFN-α7xArg were (3.7 ± 0.2) × 106 U ml−1 and (3.5 ± 0.4) × 106 U ml−1 at 2 dpi in Rachiplusia nu larvae and (1.1 ± 0.2) × 106 U ml−1 and (1.0 ± 0.15) × 106 U ml−1 at 5 dpi in Spodoptera frugiperda larvae respectively. R. nu was a better host for FeIFN-α7 and FeIFN-α7xArg expression. The 8xArg tag did not affect the biological activity of FeIFN-α7 and was useful to promote the FeIFN-α7xArg adsorption on ion exchange chromatography (IEC), allowing its purification in a single step from supernatant culture and R. nu larvae. FeIFN-α7xArg was purified from the larval extract with a yield of 70% and a purification factor of 25 free of viruses. We conclude that R. nu larvae are new low-cost hosts for the expression of recombinant FeIFN-α7. | |
dc.language | eng | |
dc.publisher | Elsevier | |
dc.relation | info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1359511314001779 | |
dc.relation | info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.procbio.2014.03.013 | |
dc.rights | https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ | |
dc.rights | info:eu-repo/semantics/restrictedAccess | |
dc.subject | FELINE INTERFERON | |
dc.subject | EXPRESSION | |
dc.subject | BACULOVIRUS | |
dc.subject | POLYARGININE TAG | |
dc.subject | PURIFICATION | |
dc.subject | ION EXCHANGE CHROMATOGRAPHY | |
dc.title | Expression and purification of recombinant feline interferon in the baculovirus-insect larvae system | |
dc.type | Artículos de revistas | |
dc.type | Artículos de revistas | |
dc.type | Artículos de revistas | |