| 茯苓多糖结构修饰及其与AA相互作用机理的研究 |
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| 引用本文： | 高贵珍,焦庆才,李绪亮,钱玉梅. 茯苓多糖结构修饰及其与AA相互作用机理的研究[J]. 激光生物学报, 2005, 14(3): 228-232 |
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| 作者姓名： | 高贵珍 焦庆才 李绪亮 钱玉梅 |
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| 作者单位： | 宿州学院生化分析实验室,中国,安徽,宿州,234000;南京大学生命科学学院,药物生物技术国家重点实验室,中国,江苏,南京,210093;南京大学生命科学学院,药物生物技术国家重点实验室,中国,江苏,南京,210093;宿州学院生化分析实验室,中国,安徽,宿州,234000 |
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| 基金项目： | 安徽省高校教学研究重点项目(JYXM2003056) |
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| 摘 要： | 将茯苓多糖硫酸化得到硫酸化茯苓多糖(SP),应用光谱法研究了SP与天青A(AA)相互作用机理,并通过理论模型测得SP与AA最大结合数N=62,结合常数K=3.703×105。考察了反应体系中AA/SP摩尔比、NaCl、乙醇、羟丙基β环糊精以及TritonX 100对相互作用的影响。并对SP与AA相互作用机理提出了合理的解释。
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| 关 键 词： | 硫酸化茯苓多糖 天青A 光谱法 最大结合数 |
| 文章编号： | 1007-7146(2005)03-228-05 |
Structural Modification of Pachymaran and the Mechanism Interaction between Azur A |
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| GAO Gui-zhen,JIAO Qing-cai,LI Xv-liang,QIAN Yu-mei. Structural Modification of Pachymaran and the Mechanism Interaction between Azur A[J]. ACTA Laser Biology Sinica, 2005, 14(3): 228-232 |
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| Authors: | GAO Gui-zhen JIAO Qing-cai LI Xv-liang QIAN Yu-mei |
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| Affiliation: | GAO Gui-zhen~ |
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| Abstract: | Pachymaran sulfated into sulfation pachymaran(SP), The mechanism of the interaction between sulfation pachymaranand and AzurA(AA) was studied by absorption spectra. The maximum binding number (N=62) and the binding equilibrium constant (K=3.703×10~5) of the sulfation pachymaran and Azur A were obtained by the exoterica model. The influence of the molar ration of AA/SP、NaCl、ethanol、hydroxypropyl-β-cyclodextrin and triton X-100 on the spectra of AA-SP complex was investigated. The mechanism of the interaction between the sulfation pachymaran and AzurA has been explained. |
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| Keywords: | sulfation pachymaran azur A spectrometry maximum biding number |
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