Archives of Pharmacal Research
- Volume 6 Issue 1
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- Pages.55-62
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- 1983
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- 0253-6269(pISSN)
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- 1976-3786(eISSN)
Drug-biomacromolecule interaction IV
- Kim, Chong-Kook (College of Pharmacy, Seoul National University) ;
- Yang, Ji-Sun (College of Pharmacy, Seoul National University) ;
- Lim, Yun-Su (College of Pharmacy, Seoul National University)
- Published : 1983.06.01
Abstract
Binding of six cephalosporins (cefotaxime, cefuroxime, cefazoline, cephalothin, cephaloridine, cephacetrile) to bovine 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-sulfonate (ANS) was used as the fluorescence probe. 2-(4'-hydroxybenzeneazo) benzoic acid(HBAB) was employed as the UV spectrophotometric probe. Compentitive bindings between cephalosporins and probes were observed. The number of binding sites of bovine serum albumin for each cephalcsporin is 2. Among six cephaloporins, cefotaxime has the highest binding constant followed by cafazoline, cefuroxime, cephalothin, cephaloridine and cephacetrile.
Keywords
- Cefotaxime;
- Cefazoline;
- Cefurexime;
- Cephalothin;
- Cephaloridine;
- Cephacetrile;
- Bovine serum albumin;
- 1-Anilinonaphthalenc-8-sulfonate (ANS);
- 2-(4′-Hydroxybenzeneazo) benzoic acid(HBAB);
- Fluorescence probe technique;
- Difference spectra