Origin of rice protein hydrolysates added to protein-free media alters secretion and extracellular proteolysis of recombinant interferon-γ as well as CHO-320 cell growth
| Autor: | Yves-Jacques Schneider, Chantal Peeters-Joris, Johann Mols, Spiros N. Agathos |
|---|---|
| Rok vydání: | 2004 |
| Předmět: |
medicine.medical_treatment
Proteolysis Bioengineering CHO Cells Biology Applied Microbiology and Biotechnology Hydrolysate Interferon-gamma Cricetinae Casein medicine Animals Plant Proteins Protease medicine.diagnostic_test Hydrolysis Chinese hamster ovary cell Oryza General Medicine Recombinant Interferon Gamma Molecular biology Cysteine protease Recombinant Proteins Biochemistry Rice protein Cell Division Biotechnology |
| Zdroj: | Biotechnology Letters. 26:1043-1046 |
| ISSN: | 0141-5492 |
| DOI: | 10.1023/b:bile.0000032960.06112.31 |
| Popis: | CHO-320 cells, cultivated in suspension in a protein-free medium supplemented with rice protein hydrolysates (peptones), secrete recombinant interferon-gamma (IFN-gamma) that undergo will or will not proteolysis, depending on the origin of the peptones. This proteolytic event, as well as the appearance of an unidentified 70 kDa gelatinase-like protease, are attributed to a cysteine protease. Casein zymographies revealed that one rice protein hydrolysate, but not another, contains a papain-like cysteine protease whose activity is undetectable in solution. This work underlines the significance of the origin of peptones when considered as supplements in serum- and protein-free media for overproduction of recombinant proteins. |
| Databáze: | OpenAIRE |
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