title: [Study on interaction of caffeine and theophylline with bovine serum albumins].
abstract: The interation of caffeine and theophylline with bovine serum albumins has been studied by fluorescence spectroscopy. The results indicated that enoxacin could bind with BSA strongly at molar ratio 1:1 and the equilibrium constants were Kc = 1.673 x 10(4) L x mol(-1) and Kt = 6.802 x 10(3) L x mol(-1), respectively. Good linear Stern-Volmer lines were observed on the fluorescence of BSA quenched by enoxacin of different concentration, indicating that the combination reaction of enoxacin with BSA is a single static quenching process.
authors.affiliation: Medical University of Shanxi, Taiyuan 030001, China.
authors.forename: Wei
authors.initials: W
authors.lastname: Bian
authors.forename: Yan-li
authors.initials: YL
authors.lastname: Wei
authors.forename: Ya-ping
authors.initials: YP
authors.lastname: Wang
authors.forename: Chuan
authors.initials: C
authors.lastname: Dong
mesh_terms: D000818:Animals; D002110:Caffeine / Q000737:chemistry*; D002417:Cattle; D000697:Central Nervous System Stimulants / Q000737:chemistry; D007700:Kinetics; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013050:Spectrometry, Fluorescence / Q000379:methods*; D013806:Theophylline / Q000737:chemistry*; D014665:Vasodilator Agents / Q000737:chemistry
chemical_list: D000697:Central Nervous System Stimulants; D014665:Vasodilator Agents; D012710:Serum Albumin, Bovine; D002110:Caffeine; D013806:Theophylline