Abstract
Abstract Gel filtration on HPLC columns can be a convenient means for the separation of soluble immune complexes from the mixture of human serum albumin (HSA)—monoclonal serum albumin antibody (Mab anti HSA). Owing to the rapidity of the method, the equilibrium is not modified, as it may be during the salting-out separation. This method has been applied to the study of the interaction between HSA and a monoclonal antibody against human immunodeficiency virus envelope protein (Mab anti HIV gp 120). Supported by the fact that HIV proteins share numerous epitopes with human proteins, a treatment to improve the specific immune response against this pathogen is proposed: it is based on the blocking of the epitopes of the self antigens, expressed in the thymus, which are in common with the virus. Repeated injections within the thymus, of neutralizing antibodies against the pathogen, obtained from a sufficiently distant animal species and purified by affinity chromatography, would prevent the T cells of the host recognizing these common epitopes from negative selection, and would improve the immune response. Moreover, the unfavourable effect of mutations within the virus genome could also be minimized by this treatment.
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