| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10843192 | Protein Expression and Purification | 2013 | 6 Pages |
Abstract
⺠A more efficient way to purify N-Flo1p from Saccharomyces cerevisiae was obtained by producing it in Pichia pastoris. ⺠The yield obtained with this organism is more than 4 times higher compared to S. cerevisiae as an expression organism. ⺠The protein was produced with a significant improvement in homogeneity of its glycosylation state. ⺠The binding activities of N-Flo1p produced by P. pastoris and S. cerevisiae are similar.
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Authors
Katty V.Y. Goossens, Henri De Greve, Ronnie G. Willaert,