Proteins are adsorbed to hydrophobic agaroses as metastable states of adsorption–desorption hysteresis These phenomena form the basis for hydrophobic phenomena form the basis for hydrophobic interaction chromatography (HIC). However, because of its complexity it has not gained the same The technique utilizes the accessible hydrophobic regions located on protein surfaces and their interactions with a weakly hydrophobic stationary phase. HIC is an excellent that modulate hydrophobic interactions. Hydrophobic interaction chromatography (HIC) is one of the basic puri-fication procedures in the biosciences. @article{FeketeHydrophobicIC, title={Hydrophobic interaction chromatography for the characterization of monoclonal antibodies and related products.}, author={Szabolcs Hydrophobic interaction chromatography (HIC) is a high-resolution technique widely used for analysis and purification of biomolecules based on differences in their hydrophobicity. In this chapter, the basic principles of HIC and theories for the retention mechanisms are addressed, as well as the main parameters to consider for the optimization Hydrophobic interaction chromatography (HIC) is one of the basic puri-fication procedures in the biosciences. However, because of its complexity it has not gained the same foothold in the methodological repertoire of protein chem-istry as has affinity chromatography or ion exchange chromatography. The salts are ordered from right to left in order of increasing “salting out” effect. A chromatographic matrix containing hydrophobic groups, binds proteins from aqueous solutions to different extents depending on the protein structures and a range of controllable factors including concentrations of salts, pH, temperature and organic solvents (Fig 2) DOI: Corpus ID: ; Hydrophobic interaction chromatography for the characterization of monoclonal antibodies and related products. This is Hydrophobic interaction chromatography is a biological recognition process corresponding to a two-dimensional lock-and-key model, that is, the dynamic pairing of a 2D key (protein) with its complementary 2D ‘lock’ (alkyl lattice).
Proteins are adsorbed to hydrophobic agaroses as metastable states of adsorption–desorption hysteresis These phenomena form the basis for hydrophobic phenomena form the basis for hydrophobic interaction chromatography (HIC). However, because of its complexity it has not gained the same The technique utilizes the accessible hydrophobic regions located on protein surfaces and their interactions with a weakly hydrophobic stationary phase. HIC is an excellent that modulate hydrophobic interactions. Hydrophobic interaction chromatography (HIC) is one of the basic puri-fication procedures in the biosciences. @article{FeketeHydrophobicIC, title={Hydrophobic interaction chromatography for the characterization of monoclonal antibodies and related products.}, author={Szabolcs Hydrophobic interaction chromatography (HIC) is a high-resolution technique widely used for analysis and purification of biomolecules based on differences in their hydrophobicity. In this chapter, the basic principles of HIC and theories for the retention mechanisms are addressed, as well as the main parameters to consider for the optimization Hydrophobic interaction chromatography (HIC) is one of the basic puri-fication procedures in the biosciences. However, because of its complexity it has not gained the same foothold in the methodological repertoire of protein chem-istry as has affinity chromatography or ion exchange chromatography. The salts are ordered from right to left in order of increasing “salting out” effect. A chromatographic matrix containing hydrophobic groups, binds proteins from aqueous solutions to different extents depending on the protein structures and a range of controllable factors including concentrations of salts, pH, temperature and organic solvents (Fig 2) DOI: Corpus ID: ; Hydrophobic interaction chromatography for the characterization of monoclonal antibodies and related products. This is Hydrophobic interaction chromatography is a biological recognition process corresponding to a two-dimensional lock-and-key model, that is, the dynamic pairing of a 2D key (protein) with its complementary 2D ‘lock’ (alkyl lattice).
Français
English
Deutsch
Español
Italiano
Português