title: Isolation of antigens and antibodies by affinity chromatography.
abstract: Antibody-antigen binding constants are commonly strong enough for an effective affinity purification of antibodies (by immobilized antigens) or antigens (by immobilized antibodies) to work out a straightforward purification method. A drawback is that antibodies are large protein molecules and subject to denaturation under conditions required for the elution from the complex. Structures of antigens can vary but usually antigens are also equally subject to similar problems. The lability of the components can sometimes make the procedure sophisticated, but usually in all cases it is possible to find a satisfactory approach. In certain cases, specific interactions of the Fc part of antibodies are more facile to exploit for their purification.
authors.affiliation: A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, 119899, Moscow, Russian Federation. vimuronets@belozersky.msu.ru
authors.forename: Vladimir I
authors.initials: VI
authors.lastname: Muronetz
authors.forename: Timo
authors.initials: T
authors.lastname: Korpela
mesh_terms: D000906:Antibodies / Q000302:isolation & purification*; D000941:Antigens / Q000302:isolation & purification*; D002846:Chromatography, Affinity / Q000379:methods*
chemical_list: D000906:Antibodies; D000941:Antigens