Download PDF by PHARMACIA FINE CHEMICALS: Affinity Chromatography: Principles and Methods

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4. Equilibrate the column with 10 column volumes of binding buffer. 5. Apply sample at a flow rate 1–4 ml/min (1 ml column) or 5 ml/min (5 ml column). Collect the flow-through fraction. A pump is more suitable for application of sample volumes greater than 15 ml. 6. Wash with 10 column volumes of binding buffer. Collect wash fraction. 7. Elute with 5 column volumes of elution buffer. Collect eluted fractions in small fractions such as 1 ml to avoid dilution of the eluate. 8. Wash with 10 column volumes of binding buffer.

Storage Wash with 5 column volumes of 20% ethanol at neutral pH and store at +4 to +8 °C. g. thrombin and trypsin, and zymogens HiTrap Benzamidine FF (high sub), Benzamidine Sepharose 4 Fast Flow (high sub) Sample extraction procedures often release proteases into solution, requiring the addition of protease inhibitors to prevent unwanted proteolysis. An alternative to the addition of inhibitors is to use a group specific affinity medium to remove the proteases from the sample. The same procedure can be used to either specifically remove these proteases or purify them.

Fraction 41 wash (manually) 45 000 Lane 6. Fraction 42 Lane 5. Fraction 3 Gua-HCl 30 000 Lane 7. Fraction 46 wash (manually) 20 100 Lane 8. Fraction 49 Lane 6. Fraction 4 Gua-HCl 14 400 wash (manually) Lane 7. Fraction 1 Urea 1 2 3 4 5 6 7 8 wash (manually) Lane 8. Fraction 2 Urea Electrophoresis: SDS-PAGE. PhastSystem, PhastGel 10–15, wash (manually) reducing conditions, 1 µl sample, Coomassie Blue staining. Fig. 27. One step refolding and purification of a (His)6-tagged recombinant protein on HiTrap Chelating HP, 1 ml, charged with Ni2+.

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Affinity Chromatography: Principles and Methods by PHARMACIA FINE CHEMICALS

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