Hydrophobic interaction chromatography of proteins on Separon hema. I. The effect of an initial salt concentration on the separation of proteins.
The influence of an initial salt concentration, phi(0), on the gradient separation of proteins using hydrophobic interaction chromatography on Separon HEMA 1000 was investigated. The results obtained were compared with the retention times and peak widths calculated according to a mathematical model.
Kleinmann
I
I
Plicka
J
J
Smídl
P
P
Svoboda
V
V
D002853:Chromatography, Liquid / Q000379:methods; D009113:Muramidase / Q000032:analysis; D009994:Osmolar Concentration; D010047:Ovalbumin / Q000032:analysis; D011506:Proteins / Q000302:isolation & purification*; D013056:Spectrophotometry, Ultraviolet; D014168:Transferrin / Q000032:analysis
D011506:Proteins; D014168:Transferrin; D010047:Ovalbumin; D009113:Muramidase