Protein Binding of Small Ions Serum Albumin

Deland, E.C.
Heirschfeldt, Rose
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RAND Corporation
Serum albumin is an especially reactive molecule, binding both positive and negative small ions, organic molecules, and even neutral molecules. As such, its role in blood biochemistry is important and pervasive. This Memorandum examines the role of serum albumin with respect to the binding of H+, C1- and Ca++. The point of view, following much of the literature, is that the Linderstrom-Lang theory--which treats the molecule as a charged sphere--can explain the anomalous behavior of serum albumin in acidity region remote from the isoionic point. But is shown, first for H+ and then for C1- and a++, that while the charged sphere concept can be stretched to fit the laboratory data, the consequent Debye-Huckel parameter bears little relation to the predicted values. The fairly exact calculations of simultaneous events possible with the computer leaves little room for doubt that a much improved theory must be developed. In fact, one conclusion is that this theory is only approximate and that an adequate explanation probably will have to begin with the exact geometry of the molecule and the consequent intramolecular interactions. This latter procedure is almost possible today--with increasing knowledge of molecular structure--whereas it was not when the farmer theory was promulgated.
ions , protein binding , mathematical model , serum albumin , Linderstrom-Lang theory