Affinity purification glycine elution chemistry - (Feb/10/2016 )
I was asked recently what the chemical mechanism of antibody/antigen elution from an affinity column via low pH glycine was. I think it's that the glycine competes with protein for binding sites, or else the disulfide bonds that allow antigen-antibody binding are reduced.
Is this correct and/or is there more detail to the story?
the glycine is used as a low pH buffer. elution is due to pH.
But can you provide more detail? What is the biochemical mechanism? Does the low pH destabilize the conformation of the antibody, protonation, or something else?
pH affects charge and conformation of proteins. both of these factors are involved in antibody-antigen interactions.
it may not fully explain the interaction(s) but you should download the "antibody purification" handbook (as well as other useful handbooks) from the ge lifesciences website: