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Molecular Weights as determined by SDS-PAGE & NATIVE PAGE GELHow do the two masses compare with one another as determined by the two methods? - If a large discrepancy is observed comparing the results of the two calculations of concentration, then what may be a biochemical reason for any (large) discrepancy?

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Sixta Kovacek
Sixta KovacekLv2
28 Sep 2019

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Related questions

A protein has a molecular mass of 200 kDa as determined by gel filtration (=native molecular weight). When separated by SDS-PAGE (without a reducing agent present) only one polypeptide appeared with a mass corresponding to 100 kDa. When determined by SDS-PAGE in combination with a reducing agent (DTT) exactly two polypeptides appeared of sizes 40 and 60 kDa. What is the correct structure of the native protein? Correct ans: The native protein is made of two 40 kDA and two 60 kDA polypeptides

Would like an explanation as to how this is correct and how similar questions would be solved

Biochemistry

Which of the following pentapeptides is expected to be the BESTdissolved in water?

Select one:

a. NH2 - ser - pro- gly - ala- cys - asn - COOH

b. NH2 - tyr - thr - gly - ser - gln - asp - COOH

c. NH2 - ser - ala - gly - phe - gln - asp - COOH

d. NH2 - gly - leu - phe - val - ser - gly - COOH

A protein has a molecular mass of 200 kDa as determined by gelfiltration (=native molecular weight). When separated by SDS-PAGE(without a reducing agent present) only one polypeptide appearedwith a mass corresponding to 100 kDa. When determined by SDS-PAGEin combination with a reducing agent (DTT) exactly two polypeptidesappeared of sizes 40 and 60 kDa. What is the correct structure ofthe native protein?

Select one:

a. The native protein is made of one 40 kDA and one 60 kDApolypeptides

b. The native protein is made of two 100 kDa polypeptides

c. The native protein is made of two 40 kDA and two 60 kDApolypeptides

d. The native protein is made of four polypeptides - two 100 kDapolypeptides, one 40 kDA and one 60 kDA polypeptides

e. None of the answers is correct.

A student given the task of purifying a protein found that the protein had a molecular mass of 400kDa when measured by gel filtration chromatography. (This technique involves the use of a column packed with material that functions like a molecular sieve. No harsh reagents are used so it preserves the native structure of the protein. ). The student wanted to confirm the purity of the protein by SDS-PAGE. When the protein was analyzed by polyacrylamide gel electrophoresis in the presence of SDS, 3 bands with the following molecular weights were obtained: 180, 160, 60kDa. However, the student realized that he/she forgot to add 2-mercaptoethanol to the sample gel buffer when it was made up. So the student ran the gel again, this time in the presence of SDS and 2-mercaptoethanol. This time, 3 bands were observed as before, however, the molecular weights were 160, 90, and 60kDa. If you were that student what would you conclude about this set of observations?

What would be the advantage of using two independent techniques (gel filtration and SDS-PAGE) to characterize a protein?

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