Literature summary extracted from
Pearce, F.G.; Griffin, M.D.; Gerrard, J.A.
Does domain swapping improve the stability of RNase A? (2009), Biochem. Biophys. Res. Commun., 382, 114-118.
General Stability
EC Number |
General Stability |
Organism |
---|
4.6.1.18 |
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
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
4.6.1.18 |
Bos taurus |
- |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
4.6.1.18 |
purification of RNase A oligomers by cation exchange chromatography |
Bos taurus |
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
4.6.1.18 |
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
EC Number |
Synonyms |
Comment |
Organism |
---|
4.6.1.18 |
ribonuclease A |
- |
Bos taurus |
4.6.1.18 |
RNase A |
- |
Bos taurus |
Temperature Stability [°C]
EC Number |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Comment |
Organism |
---|
4.6.1.18 |
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 |