Abstract
Properties of IgA in human bile were analysed by high speed liquid chromatography and radioimmunoassay in order to investigate the transport mechanism of IgA from serum into bile. IgA was found to be a predominant immunoglobulin in bile, composing approximately 50% of bile immunoglobulins. The molecular form of IgA in bile showed mainly polymeric in contrast to that of serum IgA which showed predominantly monomeric. When calculating the selectivity index of each immunoglobulin in bile, a high index was observed in polymeric IgA and IgM, whereas monomeric IgA showed a low index. In addition, nearly half of the polymeric IgA in bile had secretory component, indicating the presence of secretory IgA. These results suggest that polymeric IgA and IgM could be selectively transported from the serum into bile by the SC-mediated mechanism. However, the presence of polymeric IgA devoid of a secretory component was also detected in human bile.
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