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The binding properties of three ginsenosides, Rb1, Rc and Re, to bovine and human serum albumins have been examined by fluorescence probe technique. 1-anilinonaphthalene-8-sulfonate (ANS) was used as the fluorescence probe. Protopanaxatriol glycoside, Re, did not quench the fluorescence of ANS to the bovine serum albumin. Competitive bindings between protopanaxadiol glycosides, Rb1 and Rc, and ANS were observed. The numbers of binding sites of bovine serum albumin for Rb1 and Rc are both 3.3. The binding constants for Rb1 and Rc with bovine serum albumin were 1.91 X 104M-1 and 1.04 X 104M-1, respectively. The ginsenosides, Rb1, Rc and Re did not quench the fluorescence of ANS bound to human serum albumin.
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