Question: Design an experiment to purify protein X on an anion exchange
Design an experiment to purify protein X on an anion-exchange column. Protein X has an isoelectric point of 7.0.
Answer to relevant QuestionsWhat could be an advantage of using an anion exchange column based on a quaternary amine [i.e., resin–N+ (CH2CH3)3] as opposed to a tertiary amine [resin–NH+ (CH2CH3)2]? Distinguish between the lock-and-key and induced-fit models for binding of a substrate to an enzyme. Why is it useful to plot rate data for enzymatic reactions as a straight line rather than as a curve? Why foes the apparent KM decrease in the presence of an uncompetitive inhibitor? What are three advantages of using allosteric drugs as opposed to orthosteric ones?
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