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目的分析不同pH诱导重组人血白蛋白(Recombinant human serum albumin,rHSA)和血源人血白蛋白(Plasma-derived human serum albumin,pHSA)的构象变化。方法在不同pH值条件下,分别经紫外和荧光光谱扫描分析rHSA与pHSA及3批rHSA的二阶导数谱及275nm和295nm激发波长下的荧光光谱。结果 rHSA与pHSA的最大吸收波长均为278nm,二阶导数谱和荧光光谱均随pH值发生变化,趋势基本一致;3批rHSA的紫外和荧光光谱间无显著差异。结论 rHSA在不同pH值条件下的构象变化与pHSA基本一致,3批rHSA的构象具有良好的批间一致性。
Objective To analyze the conformational changes of pH-induced recombinant human serum albumin (rHSA) and plasma-derived human serum albumin (pHSA). Methods Under different pH conditions, the second derivative spectra of rHSA and pHSA and three batches of rHSA were analyzed by UV and fluorescence spectroscopy and the fluorescence spectra at 275 nm and 295 nm excitation wavelength respectively. Results The maximum absorption wavelengths of rHSA and pHSA were both 278 nm. The second derivative and fluorescence spectra of the two samples changed with the pH value. The trend was basically the same. There was no significant difference between the UV and fluorescence spectra of the three batches of rHSA. Conclusion The conformational changes of rHSA under different pH values are basically the same as that of pHSA. The conformations of three batches of rHSA have good batch-to-batch consistency.