Selective non-adsorption preparative chromatography of bovine immunoglobulin Gl.
Bovine immunoglobulin Gl (IgGl) was purified from blood serum by isocratic elution through a mixed-bed ion-exchange column at low ionic strength. Selection of a mobile phase pH near the isoelectric point of IgG precluded its binding to the strong cation- and anion-exchange sorbents and allowed IgGl to be eluted isocratically. Under these conditions most of the other components in the serum sample were retained on the mixed-bed column. This approach gives excellent throughput and purity.
Department of Biochemistry, Purdue University, West Lafayette, IN 47907.
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Stringham
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Regnier
D000327:Adsorption; D000818:Animals; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D007074:Immunoglobulin G / Q000302:isolation & purification*; D007202:Indicators and Reagents; D011489:Protein Denaturation
D007074:Immunoglobulin G; D007202:Indicators and Reagents