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Literature summary for 3.4.21.1 extracted from
- Stabilization of alpha-chymotrypsin upon PEGylation correlates with reduced structural dynamics (2008), Biotechnol. Bioeng., 101, 1142-1149.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bos taurus | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| additional information | chemical modification of the surface exposed lysine amino groups of alpha-CT with activated poly(ethylene glycol) | Bos taurus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| commercial preparation | - |
Bos taurus | - |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| alpha-chymotrypsin | - |
Bos taurus |
| alpha-CT | - |
Bos taurus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
thermodynamic unfolding experiments reveal that PEGylation increases the thermal transition temperature (Tm) of alpha-CT by up to 6°C and the free energy of unfolding [DELTAGU (25°C)] by up to 5 kcal/mol | Bos taurus |
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