Enantioselective binding sites on bovine serum albumin to dansyl amino acids

Yoshihiro Abe, Shikie Fukui, Yuki Koshiji, Michi Kobayashi, Tomoko Shoji, Setsuro Sugata, Hideyuki Nishizawa, Hiroshi Suzuki, Kazunori Iwata

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

The enantioselective binding sites on bovine serum albumin were examined by HPLC using 19 racemic 5-N,N-dimethylamino-1-naphthalenesulfonyl derivatives of α-amino acids (dansyl amino acids) as chiral probes. On a bovine serum albumin bonded chiral stationary phase, seven L-forms eluted faster than their D-forms, while ten D-forms eluted before their L-forms. It was speculated that either two classes or two different binding sites exist on bovine serum albumin which can be distinguished by N-dansyl-L-proline and N-dansyl-D-norvaline. This was confirmed by fluorometric experiments where non-fluorescent 1-naphthalenesulfonyl derivatives were synthesized and competitive adsorption experiments were performed. Copyright (C) 1999 Elsevier Science B.V.

Original languageEnglish
Pages (from-to)188-197
Number of pages10
JournalBiochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Volume1433
Issue number1-2
DOIs
Publication statusPublished - 1999 Aug 17

Keywords

  • Binding site
  • Bovine serum albumin
  • Dansyl amino acid
  • Fluorometry
  • High performance liquid chromatography

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology

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  • Cite this

    Abe, Y., Fukui, S., Koshiji, Y., Kobayashi, M., Shoji, T., Sugata, S., Nishizawa, H., Suzuki, H., & Iwata, K. (1999). Enantioselective binding sites on bovine serum albumin to dansyl amino acids. Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology, 1433(1-2), 188-197. https://doi.org/10.1016/S0167-4838(99)00135-1