Spurious cell surface receptors: inadequate correction for saturable, nonspecific binding mimics receptor binding.
Methods commonly used for the characterization of receptors on cell surfaces may be subject to adsorption artifacts that mimic the action of receptors even when no receptors are present. Traditional techniques such as incubation in the presence of an unrelated protein to minimize adsorption or extensive washing to eliminate nonspecific binding may be inadequate to ensure that the observed binding is due to a cell membrane--ligand interaction. In this paper three serum proteins, albumin, transferrin, and immunoglobulin G, are shown to exhibit behavior suggestive of receptor-mediated binding even in the absence of cells. Two types of control studies are suggested to establish that observed binding is attributable to interaction with cells.
Reed
R G
RG
Medical Research Institute, Mary Imogene Bassett Hospital, Cooperstown, New York 13326.
D000327:Adsorption; D000818:Animals; D001667:Binding, Competitive; D002498:Centrifugation; D005374:Filtration; D007074:Immunoglobulin G / Q000378:metabolism*; D008099:Liver / Q000378:metabolism; D051381:Rats; D011956:Receptors, Cell Surface / Q000378:metabolism*; D012709:Serum Albumin / Q000378:metabolism*; D014168:Transferrin / Q000378:metabolism*
D007074:Immunoglobulin G; D011956:Receptors, Cell Surface; D012709:Serum Albumin; D014168:Transferrin