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Literature summary for 4.6.1.18 extracted from
- Different mechanisms of action of poly(ethylene glycol) and arginine on thermal inactivation of lysozyme and ribonuclease A (2012), Biotechnol. Bioeng., 109, 2543-2552.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bos taurus | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| pancreas | - |
Bos taurus | - |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| pancreas ribonuclease A | - |
Bos taurus |
| ribonuclease A | - |
Bos taurus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
L-arginine suppresses heat-induced deamidation and beta-elimination at 98°C, resulting in the suppression of thermal inactivation of bovine pancreas ribonuclease A. Poly(ethylene glycol) with molecular weight 1000 acts as a thermoinactivation suppressor for the protein, especially at higher protein concentrations, while Arg was not effective at higher protein concentrations. Amphiphilic poly(ethylene glycol) and poly(vinylpyrolidone) inhibit intermolecular collision of thermally denatured proteins by preferential interaction with thermally denatured proteins, resulting in the inhibition of intermolecular disulfide exchange, molecular mechanism, overview | Bos taurus |
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Release 2023.1 (January 2023)
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