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Equilibrate the column with 5 ml distilled water, followed by 3 ml diluted binding buffer. 5. Apply the sample. 6. Wash with 5–10 ml diluted binding buffer until no material appears in the eluent. 7. Elute with 3–5 ml diluted elution buffer. Collect fractions into tubes containing neutralization buffer. 8. Immediately re-equilibrate the column with 5 ml diluted binding buffer. 32 Media characteristics Composition pH stability* Mean particle size HiTrap Protein G HP 2 mg/ml (MAbTrap Kit) Ligand density Ligand coupled to Sepharose HP by N-hydroxysuccinimide activation (gives stable attachment through alkylamine and ether links).
Apply the sample. 4. Wash with at least 10 column volumes of binding buffer or until no material appears in the eluent, as monitored at A280. 5. Elute the IgY with 10 column volumes of elution buffer. 6. Wash the column with 8 column volumes of wash buffer. 7. Immediately re-equilibrate the column with 5 column volumes of binding buffer. 8 M Na2SO4. The sample should have the same concentration of Na2SO4 as the binding buffer. An increase in salt concentration will reduce the purity of the eluted IgY.
45 µm filter. If needed, adjust sample conditions to the pH and ionic strength of the binding buffer either by buffer exchange on a desalting column (see page 133) or by dilution and pH adjustment. A HiTrap column can be used with a syringe, a peristaltic pump or connected to a liquid chromatography system, such as ÄKTAprime plus. 1. Equilibrate the column with 5 column volumes of binding buffer. 2. Apply sample. 3. Wash with 5–10 column volumes of the binding buffer to remove impurities and unbound material.
affinity chromatography principles and methods by GE HEalthcare