Ligandin retains and albumin loses bilirubin binding capacity in liver cytosol.
Circular dichroism methods were used to detect bilirubin-ligandin interactions in rat liver cytosol and fractions obtained at various stages during purification of ligandin. Ligandin retained its capacity to bind bilirubin in the presence of components of liver supernatant, but albumin, which binds bilirubin in serum, lost the capacity to bind bilirubin in liver supernatant. This was attributed to a greater binding specificity exhibited by ligandin. In their respective physiological milieus, albumin and ligandin are structurally adapted to bind ligands: albumin in serum, and ligandin in the cytosol of the liver cell. These studies are consistent with the hypothesis that the concentration of ligandin within the liver could regulate the net flux of certain organic anions from plasma into the liver.
D000818:Animals; D001663:Bilirubin / Q000378:metabolism*; D002942:Circular Dichroism; D003600:Cytosol / Q000378:metabolism; D005982:Glutathione Transferase / Q000378:metabolism*; D007208:Indocyanine Green / Q000378:metabolism; D008099:Liver / Q000378:metabolism* / Q000648:ultrastructure; D008297:Male; D051381:Rats; D012709:Serum Albumin / Q000378:metabolism*
D012709:Serum Albumin; D005982:Glutathione Transferase; D007208:Indocyanine Green; D001663:Bilirubin
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