Ξ±-trypsin from Bos taurus (bovine)

Enzyme Description

Extremophile
No
EC Number

Sequence

Length: 223 amino acids
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
7 measurements
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 - Ξ”HTm 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 - Ξ”HTm 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 - Ξ”HTm 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 UV–vis 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 UV–vis 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 UV–vis 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€” Ξ”HTm

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
32 measurements

Structure

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