Question

(3) The 2x sample buffer contains SDS and B-mercaptoethanol. What are their functions? (1 pt) (4) What samples would you load on the gel besides the purified plant protein? Explain your reasons for loading those samples. (2 pts) (Hint: In this lab you loaded Ladder, BEW, pool A, and pool B. Only pool B contains the purified protein, but why do we need to load all the other samples? Same principles should apply to this question for the plant protein.) Several things you might want to consider besides purifying the protein: Clone the gene coding for the protein so you can study the protein by manipulating the gene Test the effect of the protein in small animals such as mice. For example, to investigate whether this protein can prevent tumor formation in mice. If everything you've done showing the effectiveness of the protein, you may patent your finding, collaborate with a pharmaceutical company or start your own company, ask for approval to start clinical trial on human, and finally commercialize your finding. 2

Answer 1

Question 3.

SDS-PAGE (Sodium Dodecyl Sulfate PolyAcrylamide Gel Electrophoresis) of proteins that have been reduced with mercaptoethanol is useful for measuring the monomer molecular weight. Reduction of the disulfide bonds is important for allowing the protein to become completely unfolded so that it migrates properly for its molecular weight.