[Isolation and immunochemical study of monomer and dimer forms of IgA human globulins].
Monomer and dimer of myeloma IgA human globulins are isolated by means of electrophoresis, ionic exchange chromatography, gel filtration and immunoadsorbtion. They are shown to be homogenous (using analytical ultracentrifugation and immunochemical analysis) and to differ in their antigenic specificity. Dimeric form of IgA has additional antigenic determinants, which depend on the intactness of a polymer structure and which are destroyed after protein dissociation into subunits in the presence of beta-mercaptoethanol. Reconstructed polymers are polydispersed subunit aggregates, they do not have polymeric determinants inherent to native polymers.
D055598:Chemical Phenomena; D002621:Chemistry; D000939:Epitopes; D006801:Humans; D007070:Immunoglobulin A / Q000302:isolation & purification*; D046911:Macromolecular Substances; D009194:Myeloma Proteins / Q000276:immunology / Q000302:isolation & purification
D000939:Epitopes; D007070:Immunoglobulin A; D046911:Macromolecular Substances; D009194:Myeloma Proteins
Vydelenie i immunokhimicheskoe izuchenie monomernoĭ i dimernoĭ form IgA globulinov cheloveka