Affinity cleavage of cell surface antibodies using the avidin-biotin system.
In the present study, we have demonstrated the feasibility of targeting a proteolytic enzyme, via the high-affinity avidin-biotin system, to act in a highly selective manner upon a cell surface-associated antibody. As an example of this approach, a cell-bound biotinylated monoclonal antibody could be removed efficiently by means of biotinylated proteinase K, bridged to streptavidin. Only low levels of cell death were observed using this procedure. The approach may prove useful for a variety of applications, including the recovery of antibody-free positively selected cell populations.
Alon
R
R
Department of Biophysics, Weizmann Institute of Science, Rehovot, Israel.
Bayer
E A
EA
Wilchek
M
M
D000911:Antibodies, Monoclonal; D000954:Antigens, Surface / Q000737:chemistry*; D001426:Bacterial Proteins; D001710:Biotin; D002469:Cell Separation / Q000379:methods; D002470:Cell Survival; D004591:Electrophoresis, Polyacrylamide Gel; D019286:Endopeptidase K; D006801:Humans; D007124:Immunoenzyme Techniques; D011990:Receptors, Transferrin; D012697:Serine Endopeptidases; D019809:Streptavidin; D014407:Tumor Cells, Cultured
D000911:Antibodies, Monoclonal; D000954:Antigens, Surface; D001426:Bacterial Proteins; D011990:Receptors, Transferrin; D001710:Biotin; D019809:Streptavidin; D012697:Serine Endopeptidases; D019286:Endopeptidase K