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On-column cleavage of a GST fusion protein and removal of thrombin after on-column cleavage, using GSTrap FF and HiTrap Benzamidine FF (high sub). 0 - competitive elution: 20 mM p-aminobenzamidine in binding buffer - denaturing eluents: 8 M urea or 6 M guanidine hydrochloride 56 1. Equilibrate the column with 5 column volumes of binding buffer. 2. Apply the sample. 3.

3. Wash with 5–10 column volumes of the binding buffer to remove impurities and unbound material. Continue until no protein is detected in the eluent (determined by UV absorbance at 280 nm). 4. * 5. Immediately re-equilibrate with 5–10 column volumes of binding buffer. 0 per ml fraction), so that the final pH of the fractions will be approximately neutral. 35 Table 3 gives examples of some typical binding and elution conditions that have been used with Protein A Sepharose. Table 3. 0 3–4 (using thiocyanate) Binding strengths are tested with free protein A.

Reuse of HiTrap IgY Purification HP depends on the nature of the sample. To prevent cross-contamination, columns should only be reused with identical samples. Media characteristics HiTrap IgY Purification HP Ligand and density pH stability* 2-mercaptopyridine 3 mg/ml Long term 3–11 Short term 2–13 Mean particle size 34 µm *Long term refers to the pH interval over which the medium is stable over a long period of time without adverse effects on its subsequent chromatographic performance. Short term refers to the pH interval for regeneration, cleaning-in-place and sanitization procedures.

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