[Investigation on binding interaction of berberine chloride with bovine serum albumin immobilized onto chromatographic supports by frontal chromatography].
Berberine chloride (BC) is a major active constituent of coptis and can be used as an antipyrotic and antibacterial medicine. Frontal analysis was used to investigate the changes in the binding constant (K), retention factor (k), binding ratio (PPB) and mole of binding sites (m(L)) for the binding of BC on an immobilized bovine serum albumin (BSA) column at several temperatures and to obtain the thermodynamic parameters in the binding process. At 30 degrees C, the binding constant was 4.79 x 10(4) L/mol. K, k and m(L) all decreased as the temperature was increased. Among these three parameters, the change magnitude in m(L) was the most significant. It could be concluded that the decrease in the retention of BC was caused by the decrease of both K and m(L), and the change in the configuration of BSA was considered to be the main reason for the decrease of binding site. The thermodynamic analysis indicated that the main driving force for the interaction between BC and BSA is electrostatic force.
Zeng
Xiaolei
X
Department of Chemistry, Northwest University, Xi'an 710069, China. zengxiaolei@163.com
Lei
Genhu
G
Wei
Yinmao
Y
D000818:Animals; D001600:Berberine Alkaloids / Q000737:chemistry*; D002417:Cattle; D002845:Chromatography / Q000379:methods*; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013816:Thermodynamics
D001600:Berberine Alkaloids; D012710:Serum Albumin, Bovine