By Amersham Biosciences
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Example text
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. Elute with 5 column volumes of elution buffer**. 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. IgGs from most species and subclasses bind to protein G at near physiological pH and ionic strength.
3) Mix gently for 1 hour at +4 °C. Precipitation of the immune complexes 1) Add 50 µl of prepared Protein A Sepharose 4 Fast Flow or Protein G Sepharose 4 Fast Flow suspension (50% slurry). 2) Mix gently for 1 hour at +4 °C. 3) Centrifuge at 12 000 x g for 20 seconds and save the pellet. 4) Wash the pellet three times with 1 ml lysis buffer and once with wash buffer. Centrifuge at 12 000 x g for 20 seconds between each wash and discard the supernatants. Be very careful when removing the supernatants to avoid loss of the immunocomplexes.
Preparation and CIPP. Remove bulk impurities Isolate, concentrate and stabilize Step 55 Applying CIPP: Imagine the purification has three phases: Capture, Intermediate Purification and Polishing. Assign a specific objective to each step within the purification process. The purification problem associated with a particular step will depend greatly upon the properties of the starting material. Thus, the objective of a purification step will vary according to its position in the process. As shown in Figure 23, an important step for any purification is correct sample preparation and this is covered in detail in Chapter 2.