A protein is purified from a bacterium using Size Exclusion Chromatography (SEC), with a molecular weight...
A protein is purified from a bacterium using Size Exclusion Chromatography (SEC), with a molecular weight of 200kD. When this protein is run on SDS-PAGE , a sing band is observed at 100kD. Based on these observations, what can be concluded about the structure of the protein?
- The protein consist of two 200kD subiunits
- The protein has a quaternary structure
- The protein is madeup of two 100 kD subunits
- Proteins is a tetramer consisting of 200 kD domains.
- The protein contains an impurity of 100kD
WHY?
Homework Answers
C. The protein is madeup of two 100 kD subunits.
Because the results observed in SDSPAGE is 100 kDa but the protein size determined by the size exclusion chromatography is the 200 kDa. So the protein should contains two 100kDa subunits then only one band will be observed in SDSPAGE.
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