An aspiring biochemist needs some help. He is a new technician and is learning a

Question

An aspiring biochemist needs some help. He is a new technician and is learning about protein separation techniques. He has purchased some ferritin. He performs sodium dodecyl sulfate polyacrylamide electrophoresis (SDS-PAGE) on the enzyme and finds the weight to be about 18 kD. Later, he performs gel exclusion (permeation) chromatography on the enzyme in the presence of some molecular weight standards. He determines the weight of ferritin to be about 432 kD. He is confused. How would you briefly explain his finding to him? 

Explanation / Answer

the SDS-PAGE is a very denaturalizating method, so if you usesSDS-PAGE the protein will be totally denaturalizated then theweight of the protein is the exact weight of teh protein. otherwiseif you uses exclusion ( gel permeation) chromatography you donthave denaturalizating condition then the weight that you get may bethe weight corresponding to a cluster of proteins, because theproteins have interaction with other proteins such hidrogen bond ordisulfide interaction manteining the protein bonden to others.

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