I have a question to ask about the aggregation pattern of D1 and D2 proteins on
a denaturing gel electrophoresis. The mol.wt. of D1 is 32 kDa and that of D2
is around the same (may be 30 kDa). When we make a denaturing gel electrophores
is, we see two distinct bands of D1 and D2 and we also see the aggregate of the
se two proteins around 60 kDa. The question is how many aggregation patterns
that we can see taking different combinations between these two proteins in
terms of the molecular masses on the gel. Is there also a possibility that one
combination of aggregation can show varied molecular masses? If so, by how much
variation should we expect the differences in terms of molecular masses. For
For eg. D1 protein on an SDS-PAGE in my hands shows a molecular mass of 32 kDa
and the same protein in its phosphorylated form shows slightly a higher
molecular mass (around 32.5-33 kDa) on the same gel.
Any kind of suggestions, interpretations and discussion on this are most
welcome. Thanks for reading this.