化学研究
化學研究
화학연구
CHEMICAL RESEARCHES
2013年
3期
224-227
,共4页
F e3+%灯盏花素%牛血清白蛋白%相互作用
F e3+%燈盞花素%牛血清白蛋白%相互作用
F e3+%등잔화소%우혈청백단백%상호작용
Fe3+%breviscapinun%bovine serum albumin%interaction
运用荧光光谱、紫外吸收光谱探讨了Fe3＋对灯盏花素（BR）与牛血清白蛋白（BSA）相互作用的影响；从Fe3＋与BSA的静电作用、配位结合以及Fe3＋与BR的配位作用等方面分析了影响BR与BSA相互作用的因素。结果表明，Fe3＋不改变BSA与BR的作用机制，但使得二者结合的猝灭常数、结合常数及结合位点数减小。
運用熒光光譜、紫外吸收光譜探討瞭Fe3＋對燈盞花素（BR）與牛血清白蛋白（BSA）相互作用的影響；從Fe3＋與BSA的靜電作用、配位結閤以及Fe3＋與BR的配位作用等方麵分析瞭影響BR與BSA相互作用的因素。結果錶明，Fe3＋不改變BSA與BR的作用機製，但使得二者結閤的猝滅常數、結閤常數及結閤位點數減小。
운용형광광보、자외흡수광보탐토료Fe3＋대등잔화소（BR）여우혈청백단백（BSA）상호작용적영향；종Fe3＋여BSA적정전작용、배위결합이급Fe3＋여BR적배위작용등방면분석료영향BR여BSA상호작용적인소。결과표명，Fe3＋불개변BSA여BR적작용궤제，단사득이자결합적졸멸상수、결합상수급결합위점수감소。
The effect of ferric iron (Fe3+ ) on the interaction between breviscapinun (BR) and bovine serum albumin (BSA) was investigated by means of fluorescence spectrometry and ul-traviolet absorption spectrometry .The factors influencing the interaction between BR and BSA were analyzed in relation to the static action and coordination of Fe 3+ and BSA as well as the coordination action between Fe3+ and BR .Results indicate that Fe3+ does not change the mech-anism for BSA to interact with BR ,but it contributes to reduce the quenching constant ,bind-ing constant and binding sites of BSA with BR .
