Question

Explain how the same protein can migrate differently on SDS page

Answer 1

how the same protein can migrate differently on SDS page

1) The relative plenitude of positive charged amino acids like Lys and Arg will expand the authoritative of SDS particles to your protein and will build its versatility in SDS-gel.

2) Any post-translational adjustments in the potential SDS-restricting destinations like phosphorylation of Ser, Thr, and Tyr, or sulfation of Tyr (or glycosylation as specified above) will back off the portability of your protein since they will change the neighborhood hydrophobicity (or charge).

3) The nearness in your protein planning of any salts (fixations are variable) can seriously change and mutilate the versatility of your protein.

4) The nearness in your protein readiness of a few cleansers (sorts and fixations are variable) can do a similar impact in light of the fact that a considerable lot of them contend with SDS.

5) The nearness in your protein readiness of any natural arrangements (they may meddle with the authoritative of SDS with your protein).

6) The lessened or non-diminished states of your protein (as said above) may likewise influence the portability of your protein (in the event that it has some disulphide bonds).

7) Many counterfeit protein alterations, for example, biotinylation, deglycosylation, phosphorylation, cross-connecting, connection of any fluorescent marks, thus on will change the versatility of your protein.

8) For multisubunit proteins, it is vital, on the off chance that you run them with no diminishing reagent, for example, b-mercaptoethanol or DTT and without bubbling in Laemmli support, or you pursue them above conditions included. In the first case the portability of your protein will be a great deal less on the grounds that the protein will even now have it's multisubunit structure. In the second case the protein will be separated into subunits and your will see different groups speaking to every subunit.