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胰岛素分子存在形态及结构变化的同步荧光光谱研究 被引量:2

SYNCHRONOUS FLUORESCENCE SPECTROMETRIC STUDY ON THE EXISTING SPECIES AND STRUCTURAL TRANSFORMATION OF INSULIN MOLECULE
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摘要 利用同步荧光光谱技术 ,在波长差Δλ为 30nm和 80nm下对胰岛素的同步荧光光谱特征进行研究 ,发现胰岛素中的酪氨酸和色氨酸残基的同步荧光光谱随浓度改变而发生变化 ,该变化与胰岛素在溶液中的聚集状态以及浓度淬灭作用有关。当在还原剂二硫苏糖醇作用下 ,胰岛素的同步荧光峰强度和位置均发生明显的变化 。 Synchronous fluorescence spectrometric study on the existing species and the structural transformation of insulin molecule in D H buffer solution at wavelength differences (Δ λ ) of 30nm and 80nm was performed. It was found that the synchronous fluorescence spectra of tyrosine (TYR) and tryptophan (TRY), which were the residues of insulin altered with the change of insulin concentration. And when the solution was diluted, the polymer of insulin was changed into mononmer. The spectral change and the change in polymerization of insulin were found to be related to the state of aggregation and the concentration quenching effect of insulin in solution. Under the action of the reducing agent DTT added to the solution heated on a water bath at 100℃, changes in both the peak fluorescence intensities and the locations of fluorescence spectra were clearly observed. Hence the existing species and molecular structures of insulin can be characterized by the changes of synchronous fluorescence spectra.
机构地区 暨南大学化学系
出处 《理化检验(化学分册)》 CAS CSCD 北大核心 2003年第6期324-326,329,共4页 Physical Testing and Chemical Analysis(Part B:Chemical Analysis)
基金 广东省自然科学基金 (No 0 2 1190 ) 教育部科技重点项目 (No 0 0 12 4)资助
关键词 胰岛素分子 形态 结构变化 同步荧光光谱 酪氨酸 色氨酸 氨基酸残基 去折叠 Synchronous fluorescence spectrum Insulin Unfolding
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