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Literature summary for 4.6.1.18 extracted from
- Does domain swapping improve the stability of RNase A? (2009), Biochem. Biophys. Res. Commun., 382, 114-118.
General Stability
| General Stability | Organism |
|---|---|
| oligomers have similar thermal stability to that of monomeric enzyme, suggesting that the main limiting factor in RNase A stability is the tertiary, rather than quaternary structure | Bos taurus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bos taurus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| purification of RNase A oligomers by cation exchange chromatography | Bos taurus |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | oligomers have similar thermal stability to that of monomeric enzyme, suggesting that the main limiting factor in RNase A stability is the tertiary, rather than quaternary structure | Bos taurus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ribonuclease A | - |
Bos taurus |
| RNase A | - |
Bos taurus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | 70 | oligomers have similar thermal stability to that of monomeric enzyme, suggesting that the main limiting factor in RNase A stability is the tertiary, rather than quaternary structure | Bos taurus |
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Release 2023.1 (January 2023)
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