Desorption of Antigens from Disulphide-linked Immunosorbents: Recovery of Human Serum Albumin at Near Neutral pH

Abstract

IN attempts to exploit the specificity of antigen–antibody reactions for isolating antigens from mixtures, individual antigen/rabbit-antibody complexes were separated from the reaction of mixtures of antigens and corresponding mixtures of antibodies¹. Such complexes evoked in rabbits the production of monospecific antisera to the appropriate antigens². Gamma globulin preparations¹ from these sera were later rendered insoluble, either by coupling to cellulose or by polymerization through disulphide bonds, to yield specific immunosorbents which have been used to purify a required antigen in a binary mixture by removing the unwanted antigen^3,4. This communication deals with the more direct approach to antigen purification by adsorption to and subsequent desorption from its homologous immunosorbent. The problem is how to reverse the reaction of the antigen with the solid-phase antibody in conditions which will not adversely affect any biological activity of the antigen concerned.