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.
|ジャーナル||Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology|
|出版ステータス||Published - 1999 8 17|
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