https://www.onlinelibrary.wiley.com/doi/pdf/10.1002/jps.2600570601

The binding of drugs by plasma proteins.

Publisher Summary
Two striking properties stand out upon examination of the literature on plasma albumin: (1) the unusual affinity for ions, particularly anions, in which regard plasma albumin is almost in a class by itself, and (2) the remarkable degree to which the molecule is capable of undergoing extensive conformational alterations apparently in a fully reversible manner. These properties are the key to the physiological role of plasma albumin. Albumin may serve to reduce the concentration of a variety of low molecular weight ionic substances and even nonionic materials by combining with them and, thus, buffering their activity. Albumin also serves as a transport function, carrying both undesirable and desirable ions to the site of elimination or need. In a review of fatty acid transport in the blood, Frederickson and Gordon assigned an important role to albumin. The fact that organic mercurials added to blood are bound almost exclusively by the albumin component is well established. Such compounds are deposited in the kidney prior to elimination to an unloading of the albumin caused by the greater acidity of the kidney.

Chapter 6 – Plasma Albumin

Steroid-protein interactions studied by fluorescence quenching

Binding of phenytoin, L-tryptophan and O-methyl red to albumin. Unexpected effect of albumin concentration on the binding of phenytoin and L-tryptophan.

A solid-phase optoelectronic sensor for serum albumin

It has been shown that the binding capacity of dissolved serum albumin for methyl orange increases on dilution. The increased binding capacity implies a change in the protein molecule. The possible nature of this change is discussed.

HH Bauer

Papers

A polarographic investigation of the binding properties of Serum Albumin