Specific Binding of L-Tryptophan to Serum Albumin and its Function in Vivo
Many kinds of organic anions such as long-fatty acids, bilirubin, bile acids and hormones, bind to albumin in the plasma. L-Tryptophan (Trp) also binds to albumin in the plasma, and this property is quite different from those of other amino acids (Macmenamy and Oncley, 1958). Recent studies on the transport of organic anions into liver cells using perfused rat liver have suggested that ligands tightly bound to albumin rather than unbound li-gands are transferred into liver cells readily, and that hepatic uptake of ligands is primarily mediated by the direct interactions between albumin-ligand complexes and the surface of liver cells (Weisigar et al., 1981).
KeywordsOrganic Anion Left Jugular Vein Liver Cell Surface Specific Binding Ability Fresh Liver Homogenate
Unable to display preview. Download preview PDF.
- Knox, W.E., Yip, A., and Reshelf, L., 1970, L-Tryptophan 2,3-dioxygenase. in: “Methods in Enzymology 17A”, Tabor, H., and Tabor, C.W., eds., Academic Press, New York, London, pp. 415–421.Google Scholar
- Macmenamy, R.H., and Oncley, J.L., 1958, The specific binding of L-trypto-phan to serum albumin, J. Biol. Chem. 233: 1436–1447.Google Scholar
- Sasaki, E., Saito, K., Ohta, Y., Nagamura, Y., Shinohara, R., and Ishiguro, I., 1987, Facilitation of L-tryptophan uptake into rat hepatocytes by albumin, in: “Progress in Tryptophan and Serotonin Research”, Bender, D.A., Joseph, M.H., Kochen, W., and Steinhart, H., eds., de Gruyter, Berlin, pp. 377–380.Google Scholar