Immune globulin preparations such as intravenous immunoglobulin (IVIG) and monoclonal antibodies are widely used in clinics as effective therapeutic agents for the treatment of a number of autoimmune diseases, cancer, inflammations and other pathologies. Significant amounts of IgG aggregates have been found in the highly concentrated solutions of therapeutic immune proteins. The IgG self-aggregation that appears especially after prolonged storage increases the immunogenicity of the preparations and also modifies their physical properties, first of all producing the high viscosity. The attractive IgG-IgG interactions pose a significant problem for the clinical usage of the immune proteins. During last decades intensive studies of the IgG self-association were performed. The presence of IgG dimers was demonstrated in pooled preparations. These complexes are the result of idiotype-anti-idiotype interactions. In concentrated solutions of immune globulins and monoclonal antibodies self-associated IgG molecules formed a network, increasing the viscosity. The forces responsible for the IgG association are characteristic of the protein-protein interactions in general. The amino acid residues of the Fab and Fc portions participate in the IgG-IgG contacts. Recently contact residues were modified by the site-directed mutagenesis in order to decrease the formation of the IgG self-aggregates. The mutant IgG antibodies were characterized by enhanced stability as compared with the non-modified antibody molecules. Peptic pFc' fragment and the C(H)3 domain were shown to be capable of interacting with Fc regions, thus preventing IgG aggregation. In perspective both approaches could improve the formulation of immune globulin preparations. Removal of IgG aggregates could be achieved by chromatography on hydroxyapatite.