On 15 Jul 1994 15:14:16 GMT, Stephen R. Lasky wrote:
(some stuff deleted)
>In general though, we use denaturation in the presence of SDS so that a
>protein will migrate at a rate relative to its mass and not be effected by
>amino acid composition.
That's the generally accepted therory and, no doubt, many if not most
proteins fit nicely into that scheme. But there are exceptions, just one
example (might be interesting for Jean-Marc and Emma): There is a protein
called dTAF40 because on a SDS gel it has the apparent molecular mass of 40
kd. Molecular cloning of the cDNA revealed a molecular mass of only 29 kd
(Cell 75, 519-530, 1993). Could anybody kindly give an explanation for this
unusual migration on a SDS gel?
Inst. Biol. Chem.