1. Q-Sepharose @ pH 3.5, 0-0.5 M Sallt (Lowest pH condition)

2. Q-Sepharose @ pH 11, 0-0.5 M Sallt (Highest pH condition)

3. Q-Sepharose @ pH 7, 0-0.5 M Sallt (Neutral pH condition)

4. Hydrophobic Interaction, Phenyl-Sepharose CL-4B, Start ofgradient 0.5-0.0

• 2% of the enzyme activity and 0.8% of the protein haveprecipitated in the starting buffer

5. Gel filtration, Bio-Gel p-60

Exploring a more complex protein purificationexperiment

explain the answers so I gain a deeper understanding andhow did you find the pl and molecular eright of the protein(Biochem)

Write out your estimated pl and molecular weight of the protein you had to purify. Explain in one or two paragraphs how the pI and molecular weight helped choose chromatography conditions for your purification.