title: Salt-independent adsorption chromatography: new broad-spectrum affinity methods for protein capture.
abstract: The role of chromatography in capture is reviewed in terms of the special requirements imposed by the processing of very crude feedstocks. Adsorption methods which are not significantly affected by variations of feedstock ionic strength are highlighted. Methods are compared in terms of simplicity, robustness, selectivity and ease of elution. The application of such methods to enzyme and antibody purifications is summarised. Particular emphasis is placed on high ligand density methods, which have potential for broad-spectrum application.
authors.affiliation: Biochemical Recovery Group, Centre for Bioprocess Engineering, School of Chemical Engineering, University of Birmingham, Edgbaston, Birmingham B15 2TT, UK. S.C.Burton@bham.ac.uk
authors.forename: S C
authors.initials: SC
authors.lastname: Burton
authors.forename: D R
authors.initials: DR
authors.lastname: Harding
mesh_terms: D000327:Adsorption; D000906:Antibodies / Q000302:isolation & purification; D002846:Chromatography, Affinity / Q000379:methods*; D004798:Enzymes / Q000302:isolation & purification; D008024:Ligands; D011506:Proteins / Q000302:isolation & purification*; D015203:Reproducibility of Results; D012492:Salts; D012680:Sensitivity and Specificity
chemical_list: D000906:Antibodies; D004798:Enzymes; D008024:Ligands; D011506:Proteins; D012492:Salts