[Study on interaction of caffeine and theophylline with bovine serum albumins].
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.
Bian
Wei
W
Medical University of Shanxi, Taiyuan 030001, China.
Wei
Yan-li
YL
Wang
Ya-ping
YP
Dong
Chuan
C
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
D000697:Central Nervous System Stimulants; D014665:Vasodilator Agents; D012710:Serum Albumin, Bovine; D002110:Caffeine; D013806:Theophylline