Affinity Chromatography Principles and Methods Handbook
Charge Ion exchange chromatography Size Gel filtration (sometimes called size exclusion) Hydrophobicity Hydrophobic interaction chromatography Reversed phase chromatography Fig. 1. Separation principles in chromatographic purification. Affinity chromatography separates proteins on the basis of a reversible interaction between
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Superdex 75 10/300 GL and Superdex 200 10/300 GL
b3p.it.helsinki.fi11.5 0.05 M NaOH Good solubility for some compounds. Buffer additives 30% acetonitrile in For separating very hydrophobic compounds. Volatile. suitable buffer Up to 8 M urea (pH<7) Good solubility for many components. Biological activity can be maintained at lower urea contents. Certain risk for carbamylation of proteins.
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