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Binding of Aromatic Compounds to Bovine Serum Albumin

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Abstract

THE binding of non-ionic aromatic compounds to bovine serum albumin (BSA) has been approached in terms of the equilibrium between the bound and crystalline states1. The binding is quantitated in terms of the number of molecules of an aromatic compound solubilized per molecule BSA, in aqueous solution in equilibrium with the compound in its crystalline state. The measurement of this number, K, may be visualized as tantamount to the determination of the solubility of the compound in a two-dimensional solution on the surface of the protein molecule. This approach is derived from the interpretation of adsorption phenomena as thermodynamically analogous to solution phenomena2.

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Author notes

  1. M. R. V. SAHYUN

    Present address: Department of Chemistry, California Institute of Technology, Pasadena, California, U.S.A.

Authors and Affiliations

  1. National Cancer Institute, Bethesda, Maryland

    M. R. V. SAHYUN

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  1. M. R. V. SAHYUN
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SAHYUN, M. Binding of Aromatic Compounds to Bovine Serum Albumin. Nature 209, 613–614 (1966). https://doi.org/10.1038/209613a0

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