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The binding of aromatic sulphonic acids to bovine serum albumin

1968; Elsevier BV; Volume: 168; Issue: 1 Linguagem: Inglês

10.1016/0005-2795(68)90229-8

1878-1454

Michael T. Flanagan, Stanley Ainsworth,

Hemoglobin structure and function

The partitioning of several naphthylamine sulphonate derivatives between water and solutions of dodecylamine in hexane and between water and detergent micelles was studied as an aid to understanding the binding of these dyes to bovine serum albumin. The data obtained indicate that the distribution of the dyes between the two phases depends both on non-polar and electrostatic interactions. A similar dependence was found in the binding of these dyes to bovine serum albumin. Further studies with l-thyroxine and Trypan blue showed that these molecules are bound to bovine serum albumin at the sites where naphthalymaine binding occurs. The binding of Trypan blue showed interaction effects and an explanation for this is suggested in terms of a competition by the functional groups of Trypan blue for a limited number of sites.