90. A researcher purified a specific protein and performed structural analysis using two different techniques. The data are as follows: (1) Size-Exclusion Chromatography: Under native (non-denaturing) conditions, the protein elutes at a position corresponding to a molecular weight of 200 kDa; (2) SDS-PAGE (with β-mercaptoethanol): After boiling the sample in SDS and a reducing agent, a single sharp band appears at 50 kDa. Which of the following best describes the native structure of this protein?
(A) A monomeric 200 kDa protein that is non-specifically degraded into 50 kDa fragments during electrophoresis
(B) A homotetramer composed of four 50 kDa subunits held together by non-covalent interactions or disulfide bonds
(C) A homodimer composed of two 100 kDa subunits that were incorrectly measured during chromatography
(D) A heterotetramer composed of two 75 kDa subunits and two 25 kDa subunits.
(E) A 200 kDa protein that consists of a single polypeptide chain containing four internal protease cleavage sites

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統計: A(0), B(3), C(0), D(0), E(0) #3853395