The interaction between inositol and bovine serum albumin (BSA) at different temperature was investigated by means of fluorescence spectrometry. Quenching constant was obtained, and the effect of inositol on the conformation of BSA was discussed. Moreover, the shortest distance between inositol and BSA was determined based on energy transfer theory. Results show that only dynamic quenching exists between inositol and BSA.%应用荧光光谱研究了肌醇与牛血清白蛋白(BSA)分子间的相互作用;求出了猝灭常数,讨论了肌醇对BSA构象的影响,并依据能量转移理论确定了肌醇与蛋白的最近距离.结果表明,肌醇与BSA两者间的相互作用为单一的动态猝灭过程.
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