Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermomonospora sp. | - |
- |
- |
Purification (Comment) | Organism |
---|---|
TSC by ammonium sulfate fractionation, ion exchange chromatography, and gel filtration | Thermomonospora sp. |
Renatured (Comment) | Organism |
---|---|
denaturation studies using GdnCl indicate that TSC folds through a partially folded state that resembles molten globule at 1.8 M GdnCl. alpha-Crystallin chaperone-mediated in vitro folding, molecular mechanism, overview. Reconstitution of the active TSC is observed in 50 mM sodium phosphate buffer, pH 7.0, on cooling the alpha-crystallin-TSC-m complex to 4°C. Addition of alpha-crystallin to the molten globule-like intermediate of TSC complex initiates the refolding of TSC with 69% recovery of the biological activity of the enzyme | Thermomonospora sp. |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
carboxymethylcellulose + H2O | - |
Thermomonospora sp. | ? | - |
? | |
additional information | fluorescence study on interactions of chaperone alpha-crystallin with the molten globule state of the enzyme induced by guanidine hydrochloride | Thermomonospora sp. | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | fluorescence study on interactions of alpha-crystallin with the molten globule state of the enzyme induced by guanidine hydrochloride | Thermomonospora sp. |
Synonyms | Comment | Organism |
---|---|---|
1,4-beta-D-glucan glucanohydrolase | - |
Thermomonospora sp. |
Carboxymethyl cellulase | - |
Thermomonospora sp. |
TSC | - |
Thermomonospora sp. |