Investigation on the binding of tryptophan enantiomers to human serum albumin.

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The binding of radiolabelled tryptophan enantiomers to human serum albumin was investigated by ultrafiltration and by the microparticle technique. L-Trp was found to exhibit a high degree of secondary binding. D-Trp showed increased degree of binding when the HSA concentration was decreased. Stereoselective binding has also been detected in stereoselectively labelled racemic mixtures. Both L- and D-Trp were found to compete for the primary binding site with specific benzodiazepine markers. All the experiments indicate that stereoselectivity of binding is much lower than generally believed.

Original languageEnglish
Pages (from-to)237-245
Number of pages9
JournalActa biochimica et biophysica Hungarica
Issue number3
Publication statusPublished - Dec 1 1986

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry

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