Abstract

Proteins in hepatic bile from cannulated rabbits were analysed by gel filtration, electrophoresis, density gradient ultracentrifugation, and immunochemical methods. Bile-to-serum concentration ratios (no. = 8) demonstrated that IgA and free secretory component (SC) were major constituents of rabbit bile. Relative concentration ratios, obtained by dividing the bile to serum level ratio for each protein by the corresponding ratio for albumin, were 310, 1.6, 1.0, 0.82, and 0.54 for IgA, IgM, albumin, transferrin, and IgG respectively, suggesting that both IgA and IgM are selectively secreted into bile. Ligation of the bile duct (no. = 5) led to a selective increase of the serum levels of IgA and SC, the latter as secretory IgA. After intravenous injection (no. = 4) of human polymeric IgA, 37-69% of the injected dose was recovered in bile after 3 h, in contrast to 4-5% for human monomeric IgA. The active transfer of both rabbit and human polymeric IgA into rabbit bile occurs via the same hepatic SC-mediated transport process as that described for the rat.

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