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Chapter 5: Q5-9P (page 127)

Explain why a certain protein has an apparent molecular mass of 90kDwhen determined by gel filtration and 60kDwhen determined by SDS-PAGE in the presence or absence of 2-mercaptoethanol. Which molecular mass determination is more accurate?

Short Answer

Expert verified

The protein behaves like a large protein in gel filtration, resulting in a more elongated shape.

Because the mobility of the protein is denatured by SDS-coated protein, the mass under SDS-PAGE is more accurate.

Step by step solution

01

Definition of SDS-PAGE

Ulrich K. Laemmli created the discontinuous electrophoretic system known as SDS-PAGE, which is frequently employed as a technique to separate proteins with molecular masses between 5and 250kDa.

02

Step 2: Explain why a certain protein has an apparent molecular mass

In gel filtration, the protein behaves like a big protein, giving it a more elongated structure.

The mass under SDS-PAGE is more precise because protein that has been coated with SDS loses its mobility.

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Most popular questions from this chapter

Consult Table 5-1 to complete the following: (a) On a plot of absorbance at 280 nm versus elution volume, sketch the results of gel filtration of a mixture containing human cytochrome c and bacteriophage T7 RNA polymerase and identify each peak. (b) Sketch the results of SDS-PAGE of the same protein mixture showing the direction of migration and identifying each band.

(a) In what order would the amino acids Arg, His, and Leu be eluted from a carboxymethyl column at pH6 ?

(b) In what order would Glu, Lys, and Val be eluted from a diethylaminoethyl column at pH 8?

Describe the basis for separating proteins by ion exchange, hydrophobic interaction, gel filtration, and affinity chromatography.

Explain how you would use salting out to prepare a more concentrated solution of a protein.

You must cleave the following peptide into smaller fragments. Which of the proteases listed in Table 5-4 would be likely to yield the most fragments? The fewest?

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