Ξ±-trypsin from Bos taurus (bovine)
Enzyme Description
Sequence
IVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRLGEDNINVVEGNEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRVASISLPTSCASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCKSAYPGQITSNMFCAGYLEGGKDSCQGDSGGPVVCSGKLQGIVSWGSGCAQKNKPGVYTKVCNYVSWIKQTIASN
Dayanne Pinho Rosa et al. (2017)
β Determination of structural and thermodynamic parameters of bovine Ξ±-trypsin isoform in aqueous-organic media
International Journal of Biological Macromolecules
Β· doi:10.1016/j.ijbiomac.2017.03.125 β
Β· Stability - C50 Stability - deltaHTm Stability - Tm
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Database ID
UniProt: P00760 β
Sequence Annotation
Inferred - from protein name (PDB sequence from 1AQ7, correct number of residues mentionned in the publication)
Protein Source
Commercially purchased
Experimental Data (7 measurements)
7 measurements
| Property | Assay | Solvent | Solvent Volume | Aqueous Reference | Measured Value | Units | Solution | pH | Temperature | Substrate(s) | Product(s) | Cofactor(s) | Shaking | Comments |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Stability - C50 | Volume fraction of organic solvent for which 50% of the protein is in unfolded state (measured by fluorescence spectrophotometry) | Ethanol | β | β | 41.0 | % (v/v) | 50 mM glycine buffer, 20 mM CaCl2 | 3 | β | β | β | β | β | Not applicable control (in % (v/v)) |
| Stability - ΞHTm | Transition enthalpy at Tm (in kJ/mol) | Ethanol | 40% | 235.39 | 151.75 | kJ/mol | 50 mM glycine buffer, 20 mM CaCl2 | 3 | β | β | β | β | β | Classical aqueous control (in kJ/mol) |
| Stability - ΞHTm | Transition enthalpy at Tm (in kJ/mol) | Ethanol | 60% | 235.39 | 114.06 | kJ/mol | 50 mM glycine buffer, 20 mM CaCl2 | 3 | β | β | β | β | β | Classical aqueous control (in kJ/mol) |
| Stability - ΞHTm | Transition enthalpy at Tm (in kJ/mol) | Ethanol | 80% | 235.39 | 253.07 | kJ/mol | 50 mM glycine buffer, 20 mM CaCl2 | 3 | β | β | β | β | β | Classical aqueous control (in kJ/mol) |
| Stability - Tm | Melting temperature (in Kelvin) at pH 3.0 obtained by UVβvis absorption spectroscopy at 280 nm | Ethanol | 40% | 56.2 | 37.8 | Β°C | 50 mM glycine buffer, 20 mM CaCl2 | 3 | β | β | β | β | β | Classical aqueous control (in Β°C) |
| Stability - Tm | Melting temperature (in Kelvin) at pH 3.0 obtained by UVβvis absorption spectroscopy at 280 nm | Ethanol | 60% | 56.2 | 53.8 | Β°C | 50 mM glycine buffer, 20 mM CaCl2 | 3 | β | β | β | β | β | Classical aqueous control (in Β°C) |
| Stability - Tm | Melting temperature (in Kelvin) at pH 3.0 obtained by UVβvis absorption spectroscopy at 280 nm | Ethanol | 80% | 56.2 | 65.0 | Β°C | 50 mM glycine buffer, 20 mM CaCl2 | 3 | β | β | β | β | β | Classical aqueous control (in Β°C) |
Visualization : Stability β Tm
Dayanne Pinho Rosa et al. (2017)
One bar per measurement. Colour = solvent, shade = solvent volume.
Visualization : Stability β ΞHTm
Dayanne Pinho Rosa et al. (2017)
One bar per measurement. Colour = solvent, shade = solvent volume.
Visualization : Stability β C50
Dayanne Pinho Rosa et al. (2017)
One bar per measurement. Colour = solvent, shade = temperature. Hover for details.
Dayanne Pinho Rosa et al. (2021)
β Evaluation of biological activities, structural and conformational properties of bovine beta- and alpha-trypsin isoforms in aqueous-organic media
International Journal of Biological Macromolecules
Β· doi:10.1016/j.ijbiomac.2021.02.079 β
Β· Activity - Classical Stability - Tm
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Database ID
UniProt: P00760 β
Sequence Annotation
Inferred - from protein name (23 first residues from UniProt sequence absent from the mature protein)
Protein Source
Commercially purchased
Experimental Data (32 measurements)
32 measurements β page 2 of 2
| Property | Assay | Solvent | Solvent Volume | Aqueous Reference | Measured Value | Units | Solution | pH | Temperature | Substrate(s) | Product(s) | Cofactor(s) | Shaking | Comments |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Activity - Classical | Activity measured by absorbance spectrophotometry (p-nitroaniline absorbance measurement, 410 nm) in the presence of organic solvent | Methanol | 70% | 34.8 | 3.9 | Β΅M/L | 100 mM Tris-HCl buffer, 20 mM CaCl2 | 8 | 37Β°C | 0.9 mM Benzoyl-DL-arginine p-nitroanilide | N-Benzoyl-L-arginine , p-Nitroaniline | β | β | Classical aqueous control (in microM/L) |
| Activity - Classical | Activity measured by absorbance spectrophotometry (p-nitroaniline absorbance measurement, 410 nm) in the presence of organic solvent | Methanol | 80% | 34.8 | 3.8 | Β΅M/L | 100 mM Tris-HCl buffer, 20 mM CaCl2 | 8 | 37Β°C | 0.9 mM Benzoyl-DL-arginine p-nitroanilide | N-Benzoyl-L-arginine , p-Nitroaniline | β | β | Classical aqueous control (in microM/L) |
| Activity - Classical | Activity measured by absorbance spectrophotometry (p-nitroaniline absorbance measurement, 410 nm) in the presence of organic solvent | Methanol | 90% | 34.8 | 3.9 | Β΅M/L | 100 mM Tris-HCl buffer, 20 mM CaCl2 | 8 | 37Β°C | 0.9 mM Benzoyl-DL-arginine p-nitroanilide | N-Benzoyl-L-arginine , p-Nitroaniline | β | β | Classical aqueous control (in microM/L) |
| Activity - Classical | Activity measured by absorbance spectrophotometry (p-nitroaniline absorbance measurement, 410 nm) in the presence of organic solvent | Ethanol | 10% | 34.8 | 34.1 | Β΅M/L | 100 mM Tris-HCl buffer, 20 mM CaCl2 | 8 | 37Β°C | 0.9 mM Benzoyl-DL-arginine p-nitroanilide | N-Benzoyl-L-arginine , p-Nitroaniline | β | β | Classical aqueous control (in microM/L) |
| Activity - Classical | Activity measured by absorbance spectrophotometry (p-nitroaniline absorbance measurement, 410 nm) in the presence of organic solvent | Ethanol | 20% | 34.8 | 32.6 | Β΅M/L | 100 mM Tris-HCl buffer, 20 mM CaCl2 | 8 | 37Β°C | 0.9 mM Benzoyl-DL-arginine p-nitroanilide | N-Benzoyl-L-arginine , p-Nitroaniline | β | β | Classical aqueous control (in microM/L) |
| Activity - Classical | Activity measured by absorbance spectrophotometry (p-nitroaniline absorbance measurement, 410 nm) in the presence of organic solvent | Ethanol | 30% | 34.8 | 32.4 | Β΅M/L | 100 mM Tris-HCl buffer, 20 mM CaCl2 | 8 | 37Β°C | 0.9 mM Benzoyl-DL-arginine p-nitroanilide | N-Benzoyl-L-arginine , p-Nitroaniline | β | β | Classical aqueous control (in microM/L) |
| Activity - Classical | Activity measured by absorbance spectrophotometry (p-nitroaniline absorbance measurement, 410 nm) in the presence of organic solvent | Ethanol | 50% | 34.8 | 27.7 | Β΅M/L | 100 mM Tris-HCl buffer, 20 mM CaCl2 | 8 | 37Β°C | 0.9 mM Benzoyl-DL-arginine p-nitroanilide | N-Benzoyl-L-arginine , p-Nitroaniline | β | β | Classical aqueous control (in microM/L) |
| Stability - Tm | Tm measured by UV-absorption spectroscopy in the presence of organic solvent | Ethanol | 20% | 56.5 | 40.6 | Β°C | 50 mM glycine buffer, 20 mM CaCl2 | 3 | β | β | β | β | β | Classical aqueous control (in Β°C) |
| Stability - Tm | Tm measured by UV-absorption spectroscopy in the presence of organic solvent | Ethanol | 40% | 56.5 | 37.8 | Β°C | 50 mM glycine buffer, 20 mM CaCl2 | 3 | β | β | β | β | β | Classical aqueous control (in Β°C) |
| Stability - Tm | Tm measured by UV-absorption spectroscopy in the presence of organic solvent | Ethanol | 50% | 56.5 | 47.8 | Β°C | 50 mM glycine buffer, 20 mM CaCl2 | 3 | β | β | β | β | β | Classical aqueous control (in Β°C) |
| Stability - Tm | Tm measured by UV-absorption spectroscopy in the presence of organic solvent | Ethanol | 60% | 56.5 | 53.8 | Β°C | 50 mM glycine buffer, 20 mM CaCl2 | 3 | β | β | β | β | β | Classical aqueous control (in Β°C) |
| Stability - Tm | Tm measured by UV-absorption spectroscopy in the presence of organic solvent | Ethanol | 80% | 56.5 | 65.0 | Β°C | 50 mM glycine buffer, 20 mM CaCl2 | 3 | β | β | β | β | β | Classical aqueous control (in Β°C) |
Visualization : Activity β Classical
Dayanne Pinho Rosa et al. (2021)
One bar per measurement. Colour = solvent, shade = solvent volume.
Visualization : Stability β Tm
Dayanne Pinho Rosa et al. (2021)
One bar per measurement. Colour = solvent, shade = solvent volume.