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

ABSTRACT: Binding of bilirubin and of L-tryptophan to dansylated albumins was investigated. Dansylation of less than one lysine residue per molecule of albumin did not affect the bilirubin binding, but decreased the L-tryptophan binding, indicating that 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. The results indicate that, although L-tryptophan and bilirubin are bound in the same region, perhaps in a common cavity of the albumin molecule, such a cavity is sufficiently large to contain both ligands.

SUBMITTER: Jacobsen C 

PROVIDER: S-EPMC1161149 | biostudies-other | 1979 Jul

REPOSITORIES: biostudies-other