Protein Variants | Comment | Organism |
---|---|---|
E9A | site-directed mutagenesis | Bos taurus |
K66A | site-directed mutagenesis, no intramolecular bonds form in the K66A variant | Bos taurus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bos taurus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
purification of the covalent RNase A oligomers by two-step cation exchange chromatography and two gel filtration steps | Bos taurus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
commercial preparation | - |
Bos taurus | - |
pancreas | - |
Bos taurus | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
enzymatic activities of the various RNase A monomeric and zero-length or domain-swapped oligomeric species on single-stranded yeast or double-stranded poly(A)-poly(U) RNA, overview. The dimers show higher activity compared to the monomners | Bos taurus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
poly(A)-poly(U) + H2O | the enzyme dimers degrade poly(A)-poly(U) dsRNA with an activity that increases with the increase of the oligomer's basicity | Bos taurus | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | besides dimers, also trimers and higher oligomers can be identified among the products of the covalently linking reaction, and the zero-length dimers appear not to be a unique species, but heterogeneous, overview. Quantification of the zero-length oligomers | Bos taurus |
Synonyms | Comment | Organism |
---|---|---|
ribonuclease A | - |
Bos taurus |
RNase A | - |
Bos taurus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Bos taurus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5 | - |
assay at | Bos taurus |