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. 1979 Jul 1;181(1):251–253. doi: 10.1042/bj1810251

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

C Jacobsen, J Jacobsen
PMCID: PMC1161149  PMID: 486157

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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