In SDS–polyacrylamide gel electrophoresis proteins are partially denatured and separated entirely as a function of their mass
Histones are an exception; they migrate more slowly than they should, as though they are much larger than they actually are. Why does this occur?
A. Histones form dimers and tetramers, making them appear larger.
B. Histones are heavily glycosylated, greatly adding to their mass.
C. Histones have a large number of positively charged amino acid residues. The binding of SDS to the histones is not sufficient to mask these charges, resulting in slower migration.
D. Histones have an affinity for polyacrylamide.
E. Histones are somewhat insoluble, which slows their passage through the gel.
C
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