6. Which of these techniques is used to separat proteins mainly based on ma A) p

Question

6. Which of these techniques is used to separat proteins mainly based on ma A) polyacrylamide gel electrophoresis (in the 8. A fast and common method for determining the protein c ss? absence of SDS) on in column efe B) SDS-PAGE C) isoelectric focusing D) immunoblotting E) Western blotting A) tandem mass spectrometry B) salting in with ammonium sulfate C) drying a portion and weighing the sofid D) measuring light absorption at 280m. E) Edman degradation. 7. You are purifying a nuclease by affinity chromatography. To determine which fractions contain the protein of interest, you test samples of all fractions for their ability to break down DNA. This is an example of can 9. Hydrophobic interaction chr be used to separate proteins based on differences in A) ionic charge. B) solubility C) size. D) polarity. E) binding specificity. A) a binding assay. B) a biological assay. C) an enzyme assay. D) an immunological assay. E) none of the above. 10. The tripeptide "alanyl-lysyl-aspartate contains four ionizable groups with p 2.0, 3.9,9.9, and 10.5.Calculate the this molecule. C) 6.2 D) 10.2 E) none of the above

Explanation / Answer

Ans 6 B) SDS - PAGE

PAGE (Polyacrylamide Gel electrophoresis) is a technique used to seperate the proteins on the basis of size. The proteins become denatured and negatively charged with the aid of SDS, so they migrate towards anode in the gel medium and get seperated by molecular sieving effect based on their size or mass.

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