I would like to elute a biotinylated protein sample from strepavidin beads in a way that is compaticle with mass spec. I will use the EZ Biotin with the S-S link. I see that I basically have two options: 1) elute in a DTT in SDS elution buffer and then run in a gel propr to in-gel digestion, but this will lose a lot of sample
2) do an 'on-bead' trypsination i.e. don't elute at all, however I understand this can give a lot of false positives
I don't understand however, why I cannot simply elute from the beads with DTT in water. Is the S-S link not supposed to provide a method where you can elute with DTT and thus reduce the S-S bond without the harsh conditions (i.e. SDS) required for disrupting the strong bond between biotin from streptavidin. I must be missing something (or just being plain stupid).
Any advice will be greatfullt recieved