Ligandin retains and albumin loses bilirubin binding capacity in liver cytosol.
- 1 March 1978
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 75 (3) , 1213-1216
- https://doi.org/10.1073/pnas.75.3.1213
Abstract
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. The concentration of ligandin, within the liver could regulate the net flux of certain organic anions from plasma into the liver.This publication has 14 references indexed in Scilit:
- Translation in vitro of rat liver messenger RNA coding for ligandin (glutathione S-transferase B).Proceedings of the National Academy of Sciences, 1977
- Ligandin heterogeneity: Evidence that the two non-identical subunits are the monomers of two distinct proteinsBiochimica et Biophysica Acta (BBA) - Protein Structure, 1977
- Bilirubin and biliverdin binding to raty protein (ligandin)Biochimica et Biophysica Acta (BBA) - Protein Structure, 1976
- The binding of bilirubin and other organic anions to serum albumin and ligandin (Y protein).1976
- Binding of nonsubstrate ligands to the glutathione S-transferases.Journal of Biological Chemistry, 1975
- Interactions of bilirubin and other ligands with ligandinBiochemistry, 1975
- The Identity of Glutathione S -Transferase B with Ligandin, a Major Binding Protein of LiverProceedings of the National Academy of Sciences, 1974
- CIRCULAR DICHROISM STUDIES OF Y PROTEIN (LIGANDIN), A MAJOR ORGANIC ANION BINDING PROTEIN IN LIVER, KIDNEY, AND SMALL INTESTINE*Annals of the New York Academy of Sciences, 1973
- Immunological Studies of Y Protein. A MAJOR CYTOPLASMIC ORGANIC ANION-BINDING PROTEIN IN RAT LIVERJournal of Clinical Investigation, 1972
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951