Talk:Two-dimensional gel electrophoresis

From Wikipedia, the free encyclopedia

"Since the SDS molecules are negatively charged, the result of this is that all of the proteins will have approximately the same mass-to-charge ratio as each other. Next, an electric potential is again applied, but at a 90 degree angle from the first field. The proteins will be attracted to the more negative side of the gel proportionally to their mass-to-charge ratio."

If it's negatively charged, wouldn't it be attracted to the positif side instead of the negative one ?

That is exactly my concern as well.

SDS does impart a negative charge to the particle, but is then subsequently attracted to the POSITIVE pole when a charge is applied to the gel.

Also, strictly shouldn't it be size/charge not mass/charge?

The technique was introduced by Klose, 1975; O'Farrell, 1975; Scheele, 1975. Earlier publications did not include a detergent in the second dimension.

[edit] What about 2D Blue native page?

This article assumes that the only 1st dimension PAGE technique available is isoelectrofocussing; in my knowledge, there are other valid 1st dimension PAGEs which are commonly used (see: blue native PAGE, for instance). Another technique I read about in various papers (viral protein separation) used a 2D PAGE where the first dimension used a cathionic detergent. This article would greatly benefit from a broader approach.