* 1. 4 Most common salts for HIC are

* 2. You are going to purify a kinase, e.g., 6XHis-(TEV)-MBP-(3c)-PKA, describe your CIPP strategy

* 3. What is your starting salt concentration for HIC?

* 4. How many CV is usually used for gradient elution on IEX column?

* 5. An anion-exchange resin has 90 mg/ml binding capacity, how many ml of resin you should use to pack an XK25 column for gradient purification of 100 mg target protein from 900 mg protein solution with 40% purify?

* 6. After HIC purification what should be done to take care of the column?

* 7. An HIC resin has 90 mg/ml binding capacity, how many ml of resin you should use to pack an XK25 column for gradient purification of 100 mg target protein from 900 mg protein solution with 40% purify?

* 8. You have 150 ml protein solution eluted from Ni resin, the protein solution's OD280 is 1.8. The Ni elution buffer contains 0.5 M NaCl, 300 mM Imidazole, 1 mM b-ME, 10% glycerol, 20 mM Tris-HCl, pH 8.0, The next purification will be performed on an ion-exchange column (XK16/20, binding capacity 30 mg/ml). What are the necessary steps to prepare the protein solution prior to loading to the column?

* 9. You are trying to purify a DNA ligase. After homogenization and high speed centrifugation, the supernatant from E coli lysate is very viscous. What strategy will you use to reduce the sample viscosity?

* 10. Your Q FF column is very dirty. How would you clean it?
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