Monoclonal IgA was produced under serum free conditions by a murine hybridoma cell line (ZAC3) in a hollow fiber, a continuous stirred tank and a fluidized bed reactor. Differences in the antibody adsorption to DEAE chromatog. matrixes, an essential step in downstream processing, were related to the prodn. systems. Chromatog. on hydroxyapatite was used to sep. monomeric, dimeric and polymeric IgA. This method was successfully applied to IgA produced by all three reactor configurations. The binding of dimeric and polymeric IgA to antigen was tested by ELISA. Using 2-dimensional SDS-PAGE anal., dimeric IgA from the three sources was shown to be identical with respect to isoelec. points of alpha, kappa and J-chain but showed marked differences in purity. Finally the efficiency of the three bioprocesses was assessed by comparing the product yields after purifn. This included the reactor specific prodn. rates, media and time requirements and time consumption for the prodn. of 1 g purified dimeric IgA. [on SciFinder (R)]