Microcalorimetric characterization of the anion-exchange adsorption of recombinant cytochrome b₅ and its surface-charge mutants

Keyphrases

• Recombinant 100%
• Surface Charge 100%
• Adsorption 100%
• Anion Exchange 100%
• Cytochrome b5 100%
• Microcalorimetric 100%
• Adsorption Enthalpy 75%
• Differential Scanning Calorimetry 50%
• Surface Coverage 50%
• Titration 25%
• Adsorbed Proteins 25%
• Isothermal Titration Calorimetry 25%
• Ion-exchange Adsorption 25%
• Dominant Role 25%
• High Mass Loading 25%
• Single Charge 25%
• Adsorbent 25%
• Site-directed mutant 25%
• Equilibrium Adsorption Isotherms 25%
• Van't Hoff Analysis 25%
• Calorimetric Experiment 25%
• Binding Enthalpy 25%
• Adsorbed State 25%
• Entropic Effects 25%
• Free State 25%
• Adsorption Thermodynamics 25%
• Strong Anion Exchanger 25%
• Titration Calorimetry 25%

Chemistry

• Ion Exchange 100%
• Cytochrome B5 100%
• Enthalpy of Adsorption 75%
• Differential Scanning Calorimetry 50%
• Enthalpy 50%
• Adsorption Isotherm 25%
• High Performance Liquid Chromatography 25%
• Isothermal Titration Calorimetry 25%
• Calorimetry 25%

Engineering

• Ion Exchange 100%
• Enthalpy of Adsorption 100%
• Surface Coverage 66%
• Positive Value 33%
• Adsorbed Protein 33%
• Exchanger 33%
• Isothermal 33%
• Data Retention 33%
• High Performance Liquid Chromatography 33%