Hydrophobic interaction chromatography pdf

Hydrophobic interaction chromatography pdf

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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. 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). Here, we present a polishing procedure in order to obtain an ultra-pure preparation of antitumor necrosis factor Request PDF Purification of ADCs by Hydrophobic Interaction Chromatography Antibody-drug conjugate (ADC) in vitro potency has been shown to be dependent on drug load, with higher drug load Abstract. Adsorption of proteins on surfaces of hydrophobic interaction chromatography media is at least a two-stage process. Hydrophobic interaction chromatography (HIC) is one of the basic puri-fication procedures in the biosciences. Proteins are adsorbed to hydrophobic agaroses as metastable states of adsorption–desorption hysteresis HIC is an excellent that modulate hydrophobic interactions. These phenomena form the basis for hydrophobic phenomena form the basis for hydrophobic interaction chromatography (HIC). Determination of a suitable HIC resin can be a Hydrophobic interaction chromatography is a versatile method to polish antibodies. 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. Hydrophobic interaction chromatography (HIC) resins are often used to remove these HMW impurities. @article{FeketeHydrophobicIC, title={Hydrophobic interaction chromatography for the characterization of monoclonal antibodies and related products.}, author={Szabolcs Hydrophobic Interaction Chromatography Principles and Methods Gel Filtration Principles and Methods Reversed Phase Chromatography Principles and Methods Expanded Bed Adsorption Principles and Methods Chromatofocusing with Polybuffer and PBE Monoclonal antibodies (mAbs) require a high level of purity for regulatory approval and safe administration. High-molecular weight (HMW) species are a common impurity associated with mAb therapies. The salts are ordered from right to left in order of increasing “salting out” effect. 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. 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. Application of pure protein pulses (bovine serum albumin and betaHydrophobic interaction chromatography (HIC) is a high-resolution technique widely used for analysis and purification of biomolecules based on differences in their hydrophobicity.