Enantioselective binding sites on bovine serum albumin to dansyl amino acids
| Autor: | Yuki Koshiji, Shikie Fukui, Hideyuki Nishizawa, Tomoko Shoji, Yoshihiro Abe, Kazunori Iwata, Michi Kobayashi, Setsuro Sugata, Hiroshi Suzuki |
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| Rok vydání: | 1999 |
| Předmět: |
Proline
Biophysics Serum albumin Stereoisomerism Binding Competitive Biochemistry High-performance liquid chromatography Naphthalenesulfonates Structural Biology Valine polycyclic compounds Amino Acids Bovine serum albumin Binding site Molecular Biology Chromatography High Pressure Liquid Dansyl Compounds chemistry.chemical_classification Binding Sites Chromatography biology Enantioselective synthesis Serum Albumin Bovine Amino acid Spectrometry Fluorescence chemistry biology.protein Warfarin |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1433:188-197 |
| ISSN: | 0167-4838 |
| DOI: | 10.1016/s0167-4838(99)00135-1 |
| Popis: | The enantioselective binding sites on bovine serum albumin were examined by HPLC using 19 racemic 5-N, N-dimethylamino-1-naphthalenesulfonyl derivatives of alpha-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. |
| Databáze: | OpenAIRE |
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