천연색소 Brazilin 및 Hematoxylin의 BSA에 대한 결합 특성을 fluorescence probe 법을 이용하여 측정하였다. Brazilin 및 Hematoxylin은 BSA에 대해 강한 결합 친화력을 보였으며 Hematoxylin은 Brazilin 보다 더 강한 결합력을 보였다. Brazilin 및 Hematoxylin의 농도 증가에 따라 결합상수는 감소하였으며, 이는 probe-단백 결합체와 양화합물간의 상호작용 또는 Probe와 양화합물간의 결합체 형성에 기인하는 것으로 추정되었다. 양화합물과 BSA의 결합은 pH 및 이온강도에 의존적이었으며, 이 결합에는 electrostatic force 및 hydrophobic force 가 관여하는 것으로 추정되었다.
In order to investigate the protein binding characteristics of braD6n and hematoxy6n to bovine semm albumin (BSA), the fluorescence probe method was adopted. Brazilin and hematoxy6n showed strong binding affinity for BSA. It was also confirmed that hematoxy6n was bound to BSA stronger than braDlin. The association constants were decreased by the elevation of concentrations of brazilin and hematoxylin. It might be due to the complex formation of the probe and both compounds or the interaction between the probe-protein complex and both compounds. The bindings between both compounds and BSA were dependent on pH and ionic strength. It seems that electrostatic force as weD as hydrophobic force is involved in the binding of braD6n and bematoxylin to BSA.
