Investigation on the binding of tryptophan enantiomers to human serum albumin

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. Stereos...

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Bibliographic Details
Published inActa biochimica et biophysica Hungarica Vol. 21; no. 3; p. 237
Main Authors Fitos, I, Simonyi, M
Format Journal Article
LanguageEnglish
Published Hungary 1986
Subjects
Binding Sites
Binding, Competitive
Humans
In Vitro Techniques
Kinetics
Serum Albumin - metabolism
Stereoisomerism
Tryptophan - metabolism
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Summary: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.
ISSN:0237-6261