Sc. Burton et Drk. Harding, HYDROPHOBIC CHARGE INDUCTION CHROMATOGRAPHY - SALT INDEPENDENT PROTEIN ADSORPTION AND FACILE ELUTION WITH AQUEOUS BUFFERS, Journal of chromatography, 814(1-2), 1998, pp. 71-81
Citations number
27
Categorie Soggetti
Chemistry Analytical","Biochemical Research Methods
A new form of protein chromatography, hydrophobic charge induction, is
described. Matrices prepared by attachment of weak acid and base liga
nds were uncharged at adsorption pH. At low ligand densities, protein
adsorption was typically promoted with lyotropic salts. At higher liga
nd densities, chymosin, chymotrypsinogen and lysozyme were adsorbed in
dependently of ionic strength. A pH change released the electrostatic
potential of the matrix and weakened hydrophobic interactions, inducin
g elution. Matrix hydrophobicity and titration range could be matched
to protein requirements by ligand choice and density. Both adsorption
and elution could be carried out within the pH 5-9 range. (C) 1998 Els
evier Science B.V. All rights reserved.