High-performance liquid chromatography of proteins on compressed, non-porous agarose beads. II. Anion-exchange chromatography.
Macroporous agarose beads were rendered impermeable to proteins by shrinkage and cross-linking in organic solvents. The chromatographic properties of compressed beds of these non-porous beads derivatized for high-performance ion-exchange chromatography were studied, e.g., the resolution as a function of gradient time, flow-rate (at constant gradient volume) and loading capacity. The columns permit high flow-rates and the resolution is about the same at low and high flow-rates. The beads are stable up to pH 14.
Liao
J L
JL
Institute of Biochemistry, University of Uppsala, Sweden.
Hjertén
S
S
D000818:Animals; D000837:Anion Exchange Resins; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D003432:Cross-Linking Reagents; D004852:Epoxy Compounds; D006736:Horses; D009124:Muscle Proteins / Q000302:isolation & purification; D020005:Propanols; D011506:Proteins / Q000302:isolation & purification*; D012685:Sepharose
D000837:Anion Exchange Resins; D003432:Cross-Linking Reagents; D004852:Epoxy Compounds; D009124:Muscle Proteins; D020005:Propanols; D011506:Proteins; D012685:Sepharose; C004312:glycidol