Dansylation of human serum albumin in the study of the primary binding sites of bilirubin and l-tryptophan

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Abstract
The binding of bilirubin and L-tryptophan to dansylated albumins was investigated. Dansylation of less than 1 lysine residue per molecule of albumin did not affect the bilirubin binding but decreased the L-tryptophan binding; dansylation had taken place in or near the L-tryptophan-binding site. Native albumin and albumin-bilirubin 1:1 complex showed the same affinity for L-tryptophan. L-tryptophan and bilirubin are bound in the same region, perhaps in a common cavitiy of the albumin molecule; such a cavity is apparently large enough to contain both ligands.