A protein was purified to homogeneity. Determination of the mass by gel-filtration chromatography yields 60 kDa....

A protein was purified to homogeneity. Determination of the mass by gel-filtration chromatography yields 60 kDa. Chromatography in the presence of 6 M urea yields a 30-kDa species. When the chromatography is repeated in the presence of 6 M urea and 10 mM β-mercaptoethanol, a single molecular species of 15 kDa results. Which of the following best describes the structure of the protein? A. a dimer of 30 kDa subunits linked by disulfide bonds B. a tetramer of 15 kDa subunits with all subunits linked to each other by disulfide bonds C. a tetramer of 15 kDa subunits with two subunits forming 30 kDa dimers through disulfide bonds D. a tetramer of 30 kDa subunits linked by disulfide bonds E. none of the above

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queen_honey_blossom answered 1 year ago

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