Practice question

MCQ

Question

Electrophoresis of a purified protein in SDS-PAGE in the presence of 2- mercaptoethanol yields two bands of 35 kDa and 45 kDa. However, in a gel filtration chromatography, the same protein elutes as 80 kDa. What conclusion will you draw from the results?

Options

Choose one · Correct answer highlighted

The protein is not purified to homogeneity. Two bands generated in SDS-PAGE due to degradation. The protein is a homodimer The protein is a heterodimer Correct

Explanation

Mechanistically, enzyme catalysis and lipid structure involves substrate affinity, transition state stabilization and phospholipid composition govern function. This validates The protein is a heterodimer because it reflects catalytic efficiency and membrane organization, a pattern repeatedly demonstrated in biochemistry research.

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