[Fluorescence study on the interaction of alizarin yellow R and bovine serum albumin in alkali solution].
The interaction of alizarin yellow R(AYR) and bovine serum albumin (BSA) was investigated by fluorescence method in alkali buffer solution. It was shown that AYR had a powerful ability to quench the BSA fluorescence at excitation and emission wavelengths of lambda(ex) = 393 nm and lambda(em) = 641 nm in the medium solution of pH 11.00, and there were five binding sites of AYR to BSA; The combination reaction of AYR with BSA was a static quenching process, and from the effects of temperature on the fluorescence quenching rate of AYR-BSA and the Stern-Volmer quenching constant (K(SV)) and the Lineweaver-Burk quenching constant (K(LB)), the binding constant was calculated to be K = 1.6 x 10(4) L x mol(-1); as the enthalpy change deltaH(theta) < 0 and entropy change deltaS(theta) < 0, and AYR has an ability to quench the BSA-CBBG fluorescence, it can be deduced that the Van der Walls force and hydrogen bond are the main binding forces between AYR and BSA.
Zhang
Huan
H
Institute of Chemistry, Southwest University of Science and Technology, Mianyang 621010, China.
Wang
Xing-Ming
XM
Wang
Qing-Cheng
QC
Shi
Rong-Ming
RM
Ding
Li-Sheng
LS
D000468:Alkalies / Q000737:chemistry; D000818:Animals; D001391:Azo Compounds / Q000737:chemistry* / Q000378:metabolism; D002417:Cattle; D004396:Coloring Agents / Q000737:chemistry* / Q000378:metabolism; D005453:Fluorescence; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D015394:Molecular Structure; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000737:chemistry* / Q000378:metabolism; D012996:Solutions / Q000737:chemistry; D013050:Spectrometry, Fluorescence / Q000379:methods*; D013816:Thermodynamics
D000468:Alkalies; D001391:Azo Compounds; D004396:Coloring Agents; D012996:Solutions; C549930:alizarin yellow R; D012710:Serum Albumin, Bovine