Purification and characterization of chimeric human IgA1 and IgA2 expressed in COS and Chinese hamster ovary cells.

摘要: Ag-specific chimeric human IgA molecules, of the two subclasses, IgA1 and IgA2, have been expressed in mammalian cell systems. Analysis secreted purified milligram quantities from stable Chinese hamster ovary transfectants by Ag affinity chromatography, has allowed a direct comparison biologic properties subclasses. HPLC gel filtration analysis revealed that both molecules associate predominantly into dimers. The monomer units are presumed to interact noncovalently, inasmuch as no dimers evident when antibodies subjected SDS-PAGE. recombinant glycosylated, lectin blotting procedure H chains subclasses recognized Con A. When digestion preparations IgA1-specific proteases pathogenic streptococcal strains, Streptococcus sanguis oralis, behave just their natural equivalents. Thus, only molecule is cleaved, with IgA2 remaining intact. In terms interaction effector isotypes were shown Fc alpha receptors on calcitriol-stimulated HL-60 cells similar affinity, but neither antibody was found C1q. expression system described readily permits manipulation genes, which should lead fuller molecular understanding how this important mediates its function.