Question: In isoelectric focusing, proteins are separated on the basis of their [A]. relative content of positively charged residue only [B]. relative content of negatively charged residue only [C]. size [D]. relative content of positively and negatively charged residue Answer:…

Question: In SDS-PAGE, the protein sample is first [A]. treated with a reducing agent and then with anionic detergent followed by fractionation by electrophoresis [B]. fractionated by electrophoresis then treated with an oxidizing agent followed by anionic detergent. [C]. treated…

Question: In an SDS-PAGE [A]. proteins are denatured by the SDS [B]. proteins have the same charge-to-mass ratio [C]. smaller proteins migrate more rapidly through the gel [D]. all of the above Answer: Option D Explanation: No answer description available…

Question: In a native PAGE, proteins are separated on the basis of [A]. net negative charge [B]. net charge and size [C]. net positive charges size [D]. net positive charge Answer: Option B Explanation: No answer description available for this…

Question: In a gel filtration column [A]. smaller proteins enter the beads more readily [B]. large proteins elute first [C]. both (a) and (b) [D]. large proteins enter the beads more readily Answer: Option C Explanation: No answer description available…

Question: Electrophoresis of histones and myoglobin under non-denaturing conditions (pH = 7.0) results in [A]. both proteins migrate to the anode [B]. histones migrate to the anode and myoglobin migrates to the cathode [C]. histones migrate to the cathode and…