Using a five-step protocol, you have purified an enzyme to the point where the specific activity remains constant when you perform any additional purification steps. When you run the purified enzyme on a gel filtration chromatography column, you find it has a molecular mass of 50 kD. However, when you run the purified enzyme on a SDS-PAGE gel, you obtain two different sized peptides one 30 kD and the other 20 kD. What could be the possible explanations for this result? (KAS)© BrainMass Inc. brainmass.com March 21, 2019, 10:57 pm ad1c9bdddf
This solution assists in interpreting the results of an enzyme purification.