[Study on the interaction of tetraiodofluorescein and bovine serum albumin by fluorimetry].
The binding reaction of tetraiodofluorescein with bovine serum albumin i n aqueous solution was studied by fluorimetry.The binding constant is 2.65 x 10(5) L x mol(-1), the equilibrium constant is 5.7 x 10(4) L x mol(-1), and the binding number is 0.86. The research results of binding model indicate that the hydrophobic force was the main binding force. The presence of BSA can increase the fluorescence intensity of TIF. And the deltaF(F-F0) is linear to the concentration of BSA in a certain range, so the first analytical application was proposed. The linear dynamic range (LDR) was 8 x 10(-7) - 9 x 10(-6) mol x L(-1), the limit of detection (LOD) was 9.88 x 10(-8) mol x L(-1), and the relative standard deviation (RSD) was 3.4%.
Li
Gai-xian
GX
Department of Chemistry, Shanxi University, Taiyuan 030006, China.
Li
Jian-qing
JQ
Wei
Yu-xia
YX
Dong
Chuan
C
D000465:Algorithms; D000818:Animals; D002417:Cattle; D005452:Fluoresceins / Q000737:chemistry* / Q000378:metabolism; D005453:Fluorescence; D005470:Fluorometry; D057927:Hydrophobic and Hydrophilic Interactions; D007700:Kinetics; D008956:Models, Chemical; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000737:chemistry* / Q000378:metabolism
D005452:Fluoresceins; D012710:Serum Albumin, Bovine