• Archives of Pharmacal Research
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• v.7 no.1
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• pp.11-15
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• 1984

Binding of sic cephalosporins (cefotaxime, cefuroxime, cafazoline, cephalothin, cephaloridine, cephacetrile) to human serum albumin was studied. Fluorescence probe technique and difference spectrophotometry were employed to evaluate the nature and degree of association of cephalosporin-albumin complex. 1-anilinonaphthalene-8-surfonate was used as the fluorescence probe, and 2-(4'-hydroxybenzeneazo)benzoic acid as the UV spectrophotometric probe. Competitive bindings between cephalosporins and probe were observed. For the binding of cephalosporins to human serum albumin, three binding sites were identified by fluorescence probe technique but four binding constants of cephalosporins to human serum albumin measured by fluorescence probe technique are higher than those meausred by UV spectrophotometry.

• Archives of Pharmacal Research
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• v.6 no.1
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• pp.63-68
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• 1983

The binding properties of three ginsenosides, Rb$_{1}$, Rc and Re, to bovine and human serum albumins have been examined by fluorescence probe technique. 1-anilinonphathalene-8-sulfonate (ANS) was used as the fluorescence probe. Protopanaxatriol glycoside, Re, did not quench the fluorscence of ANS to the bovine serum albumin. Competitive bindings between protopanaxadiol glycosides, Rb$_{1}$ and Rc are both 3.3 . The binding constants for Rb$_{1}$ and Rc with bovine serum albumin were 1.91 * 10$_{4}$M$_{-1}$ AND 1.04 * 10$^{[-994]}$ M$^{-1}$ , respectively. The ginsenosides, Rb$_{1}$, Rc and Re did not quench the fluorescence of ANS bound to human serum albumin.