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作 者:孙国章[1] 何莹 尹照瑞 黄庆玉 李凤丽[5] Sun Guozhang;He Ying;Yin Zhaorui;Huang Qingyu;Li Fengli(Tianjin Tianshili Modern Chinese Medicine Resources co.LTD,Tianjin 300193;Tianjin Yaang Pharmaceutical International Development Promotion co.LTD,Tianjin 300193;Tianjin Shitian Pharmaceutical co.LTD.,Tianjin 300193;Tianjin Tianshili Zhijiao Pharmaceutical co.LTD.,Tianjin 300193;The First Affiliated Hospital of Tianjin University of TCM,Tianjin 300193)
机构地区:[1]天津天士力现代中药资源有限公司,天津300193 [2]天津雅昂医药国际化发展促进有限公司,天津300193 [3]天津市石天药业有限责任公司,天津300193 [4]天津天士力之骄药业有限公司,天津300193 [5]天津中医药大学第一附属医院,天津300193
出 处:《山西中医药大学学报》2020年第3期192-195,共4页Journal of Shanxi University of Chinese Medicine
基 金:国家“重大新药创制”科技重大专项项目(2010ZX09102-201)。
摘 要:目的:研究灯盏花素与牛血清白蛋白相互作用的荧光猝灭类型、结合位点、结合常数和作用力类型。方法:采用紫外-可见分光光度法和荧光光谱法研究两者的相互作用,并通过计算得到相关参数。结果:通过紫外-可见分光光度法发现,在灯盏花素的作用下,牛血清白蛋白的最大吸收峰发生了轻微蓝移,蛋白质疏水性增强;通过荧光光谱法发现,灯盏花素与牛血清白蛋白作用的猝灭类型为静态-动态联合猝灭,其中静态猝灭起主导作用。通过计算热力学参数,得到两者的相互作用力主要为静电引力。结论:阐明了灯盏花素和牛血清白蛋白相互作用的机制,建立了灯盏花素和牛血清白蛋白的结合模型。Objective:To investigate the type of fluorescence quenching,the binding site,the binding constant and the type of action force,caused by the interaction between breviscapine and bovine serum albumin.Methods:The interaction between breviscapine and BSA was investigated by the UV-Vis spectrometry and fluorescence spectrometry and the related parameters were obtained by calculation.Results:It was found by UV-Vis spectrometry that the maximum absorption peak of bovine serum albumin was slightly blue shift and the hydrophobicity of protein was enhanced.It was found by fluorescence spectrometry that the quenching of breviscapine and BSA was static-dynamic joint quenching,and static-quenching played a dominant role.The interaction force between them is mainly electrostatic attraction by calculating thermodynamic parameters.Conclusion:The mechanism of the interaction between breviscapine and bovine serum albumin was clarified and the binding model of breviscapine and bovine serum albumin was established.
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