Characterization of a peptide affinity support that binds selectively to staphylococcal enterotoxin B.

作者: Guangquan Wang , Ruben G. Carbonell

DOI: 10.1016/J.CHROMA.2005.05.010

关键词: ChromatographyReaction rate constantMass transferAdsorptionLigand (biochemistry)Langmuir adsorption modelRate-determining stepChemistryPeptideDissociation constant

摘要: Abstract The influences of mass transfer and adsorption–desorption kinetics on the binding staphylococcal enterotoxin B (SEB) to an affinity resin with peptide ligand, Tyr-Tyr-Trp-Leu-His-His (YYWLHH) have been studied. bed particle porosities, axial dispersion coefficient pore diffusivity were measured using pulse experiments under unretained conditions. Adsorption isotherms for SEB YYWLHH resins densities in range from 6 220 μmol/g fitted a bi-Langmuir equation. At below 9 μmol/g above 50 μmol/g, dissociation constants lower (2 × 10−3 7 × 10−3 mol/m3), capacities larger (43–47 mg SEB/g). In 9 50 μmol/g (13 × 10−3 24 × 10−3 mol/m3) (33–37 mg These observations are consistent transition single point attachment protein ligand at low multipoint high densities. general rate (GR) model chromatography was used fit experimental breakthrough curves retained conditions determine intrinsic adsorption, which varied 0.13 0.50 m3 mol−1 s−1, exhibited no clear trend increasing density. An analysis number units various steps column indicated that film transfer, diffusion (POR) adsorption can all play important role overall step apparently being determining 50 μmol/g.

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