Burton S C, Harding D R
Department of Chemistry, Massey University, Palmerston North, New Zealand.
J Chromatogr A. 1998 Jul 24;814(1-2):71-81. doi: 10.1016/s0021-9673(98)00436-1.
A new form of protein chromatography, hydrophobic charge induction, is described. Matrices prepared by attachment of weak acid and base ligands were uncharged at absorption pH. At low ligand densities, protein adsorption was typically promoted with lyotropic salts. At higher ligand densities, chymosin, chymotrypsinogen and lysozyme were adsorbed independently of ionic strength. A pH change released the electrostatic potential of the matrix and weakened hydrophobic interactions, inducing 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.
本文描述了一种新型蛋白质色谱法——疏水电荷诱导色谱法。通过连接弱酸和弱碱配体制备的基质在吸附pH值下呈电中性。在低配体密度时，促溶盐通常会促进蛋白质吸附。在高配体密度时，凝乳酶、胰凝乳蛋白酶原和溶菌酶的吸附与离子强度无关。pH值的变化释放了基质的静电势并削弱了疏水相互作用，从而诱导洗脱。通过配体的选择和密度，可以使基质的疏水性和滴定范围与蛋白质需求相匹配。吸附和洗脱均可在pH 5 - 9范围内进行。
