| Autor: |
E V, Morozkina, E A, Vavilova, S S, Zatsepin, E V, Klyachko, T A, Yagudin, A M, Chulkin, I V, Dudich, L N, Semenkova, I V, Churilova, S V, Benevolenskii |
| Rok vydání: |
2016 |
| Předmět: |
|
| Zdroj: |
Prikladnaia biokhimiia i mikrobiologiia. 52(2) |
| ISSN: |
0555-1099 |
| Popis: |
A system for the production of mutant recombinant human alpha-fetoprotein (rhAFPO) lacking the glycosylation site has been engineered in the yeast Pichia pastoris. A strain of the methylotrophic yeast Pichia pastoris GS 115/pPICZ?A/rhAFP0, which produces unglycosylated rhAFPO and secretes it to the culture medium, has been constructed. Optimization and scale-up of the fermentation technology have resulted in an increase in the rhAFP0 yield to 20 mg/L. A scheme of isolation and purification of biologically active rhAFP0 has been developed. The synthesized protein has the antitumor activity, which is analogous to the activity of natural human embryonic alpha-fetoprotein. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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