Monensin and bile protein secretion. A tool to investigate hepatocyte intracellular vesicular polarity.

Bile derived from monensin treated bile-fistula rats was analysed by SDS-polyacrylamide gels. Differences in proteins were observed for bands presumptively corresponding to transferrin, secretory-IgA and free secretory components after treatment with the ionophore. The results show that the secretion of proteins in bile is differentiated and asyncronous, confirming a polarity of the hepatocyte subcellular compartments.