Ligand binding albumin

J. R. Brown, R Shockley, Serum Albumin Structure and Characterization of Its Ligand Binding Sites , in Lipid-Protein Interactions , Eds. P. C. Jost, O. H. Griffith, Wiley, New York, 1982, Vol. 1, p. 25-68. 

Good overall agreement was obtained in the conclusions reached on folding-by-parts in albumin by immunochemical (Teale and Benjamin, 1976, 1977) and small ligand binding measurements (Johanson et al., 1977, 1981). This serves to increase our confidence in the usefulness of immunochemical approaches to this kind of problem. 

King, T. P. and Spencer, E. M. 1970. Structure studies and organic ligand-binding properties of bovine plasma albumin. J. Biol. Chem. 245, 6134-6148. 

Extensive research on albumin has led to an increasingly clear picture of ligand binding. The dye phenol red has been widely used as a model for the binding of natural ligands to proteins. Experimental results have shown that each molecule of albumin binds at least six molecules of phenol red. The presence of fatty acids such as decanoate, palmitate, stearate, and oleate... 

Kragh-Hansen U (1990) Structure and ligand binding properties of human serum albumin. Dan Med Bull 37(l) 57-84... 

Ligand-induced conformational changes in the protein can result in both cooperative and antagonistic binding effects on other ligands binding to the same protein. An example of a cooperative interaction is the enhancement of the interactions of progesterone and testosterone with human serum albumin (HSA) by the palmitate ion. 

We report here the C2N2 treatment of RNase S which traps a minor conformer restoring some of the properties of RNase A, and of serum albumin where C2N2 locks in a low a - helix form and alters ligand binding. 

U. Kragh-Hansen, Molecular aspects of ligand binding to senim albumin, Pharmacol. Rev., 33 17 (1981). 

Often utilized as a substitute for a typical protein, albumin needs no introduction to the protein chemist. Because of its availability, low cost, stability, and unusual ligand-binding properties, serum albumin has been one of the most extensively studied and applied proteins in biochemistry. However, as a protein, albumin is far from typical, and the widespread interest in and application of albumin have not been balanced by an understanding of its molecular structure. Indeed, for more than 30 years structural information was surmised based solely on techniques such as hydrodynamics, low-angle X-ray scattering, and predictive methods. 

Fig. 21. Illustration summarizing the various ligand-binding sites on serum albumin. The asterisks denote binding sites that can be inferred all others have been determined crystallographically.

---