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1.
探讨了铌-铬天青S配合物与牛血清白蛋白(BSA)结合反应体系.在pH 4.6的邻苯二甲酸氢钾-NaOH(Clark-Lubs)缓冲溶液中,在OP存在下,铌-铬天青S配合物与牛血清白蛋白进一步形成复合物,其最大吸收峰位于595 nm,且随着BSA量的增加,体系在595 nm波长处吸收峰也随着增大.据此建立以铌-铬天青S配合物为光谱探针,分光光度法测定蛋白质含量的新方法.牛血清白蛋白含量在0~0.32 mg/mL的范围内符合比尔定律,摩尔吸光系数ε595为 4.4×105 L·mol-1·cm-1,相关系数为γ=0.9996,生物体内的常见物质基本上不干扰测定,方法可用于人血清蛋白中蛋白质的测定.  相似文献   

2.
铬天青S的液/液界面离子转移过程   总被引:2,自引:0,他引:2  
孙志胜  汪尔康 《化学学报》1989,47(7):644-649
本文研究了酸性染料显色剂铬天青S的液/液界面离子转移行为, 用循环伏安法和电流扫描计时电位法研究了铬天青S在水/硝基苯和水/1,2-二氯乙烷两种界面上的离子转移过程, 根据铬在青S在溶液中的离解平衡和电化学性质, 讨论了界面离子转移机理,研究了基础电解质和溶剂对铬天青S转移性能的影响, 在Britton-Robinson缓冲溶液中测得半波电位PH曲线与理论公式相一致, 由本法所得离解常数与文献值接近, 计算了转移离子的标准转移电位和标准吉布斯转移能。  相似文献   

3.
蛋白质与铁(Ⅲ)-铬天青S结合反应的研究   总被引:7,自引:0,他引:7  
蛋白质与铁(Ⅲ)-铬天青S结合反应的研究魏永巨,李克安,童沈阳(北京大学化学系,北京,100871)关键词血清白蛋白;γ-球蛋白;铁(Ⅲ)-铬天青S配合物;吸收光谱某些金属配合物与蛋白质的结合反应已被用于蛋白质的定量分析[1~4]。我们用吸收光谱法研...  相似文献   

4.
由于胶束增溶三元络合物的应用日益增长,表面活性剂作用机理的研究显得越来越重要了。人们在这领域已进行了许多研究,如西田宏的拟均相萃取理论;小原人司的电荷集合体电场吸附模型;萨文的单分子作用理论等等。尤其值得注意的是慈云祥等最近提出的协同微扰理论,认为金属离子和表面活性剂作为两个电场,从铬天青S分子两端靠近,对铬天青S分子产生协同微扰,从而造成铬天青S分子完全去质子化。  相似文献   

5.
关于微量铝的测定,目前以铬天青S分光光度法比较成熟,应用较广。与其他测定铝的显色剂比较,铬天青S具有灵敏度高、选择性好的优点。能否适用于稀土氧化物中微量铝的测定过去未见报导。为适应当时提取高纯氧化钇试验的需要,我们拟定了此方法。采用草酸沉淀分离大量稀土,然后用高氯酸冒烟破坏草酸,在pH5.7左右使铝和铬天青S生成红色络合物,用抗坏血酸还原铁(Ⅲ),用盐酸羟胺络合残余稀土,借此测定微量铝。 1.仪器:国产72型分光光度计。  相似文献   

6.
本文根据铜(Ⅱ)与铬天青S(CAS)在有过量的氯化十四烷基二甲基苄基铵存在下可形成稳定红色络合物,从而研究了铜(Ⅱ)与铬天青S在有过量的氯化十六烷基吡啶(CPC)存在下的显色反应条件。实验部分(一)试剂与仪器  相似文献   

7.
蛋白质与酸性铬蓝K相互作用的分光光度研究   总被引:10,自引:0,他引:10  
朱铿  童沈阳 《化学学报》1996,54(6):620-624
本文研究了不同酸度下, 酸性铬蓝K与牛血清白蛋白的作用情况。用光度法求出了不同条件下酸性铬蓝K与牛血清白蛋白的结合个数或结合常数, 并用三种不同的方法相互进行对照。证明酸性铬蓝K在牛血清白蛋白上有两类不同结合部位。  相似文献   

8.
近年来,胶束增溶分光光度法发展较快。利用该法测定稀土的报导亦日见增多。我们曾用溴化辛基三甲铵(简写作C_8NBr)和硫酸辛酯钠(简写作NaC_8S)作为铬天青S  相似文献   

9.
本文用极谱法和循环伏安法研究了铬天青S和电还原。在Britton-Robinson缓冲溶液中,在PH_(4—11)时,铬天青S可产生两个受扩散控制的一电子还原波。其中第一波(峰)相当于由氧化态还原为中间态;第二波(峰)相当于由中间态不可逆地还原为还原态。根据实验结果提出了电还原机理。  相似文献   

10.
本文研究了铬天青SL(CAS)与牛血清白蛋白(BSA)在酸性溶液中反应前后的吸收光谱,认为CAS 与BSA 主要通过静电引力而结合,研究发现这一探针反应不符合Scatchard模型,提出了处理此类体系溶液平衡的一个新的线性回归方程, 由此方程可以求算结合常数,最大结合数以及吸光系数等体系参数,最后考察了实验条件对结合反应的影响.  相似文献   

11.
阿霉素与牛血清白蛋白结合作用的研究   总被引:65,自引:5,他引:60  
黄波  邹国林  杨天鸣 《化学学报》2002,60(10):1867-1871
结合荧光光谱和吸收光谱研究了阿霉素与牛血清白蛋白间的结合作用,确定了 阿霉素对牛血清白蛋白的荧光猝灭过程的猝灭机理,测定了不同酸度条件下该结合 反应的结合常数、结合位点数,依据能量转移理认确定了药物和蛋白间的结合距离 。通过比较阿霉素和去糖基阿霉素与牛血清白蛋白的相互作用,结合阿霉素对蛋白 构象的影响,讨论了药物与蛋白的结合模式。  相似文献   

12.
The interaction between bovine serum albumin (BSA) and pegylated puerarin (Pur) in aqueous solution was investigated by UV-Vis spectroscopy, fluorescence spectroscopy and circular dichroism spectra (CD), as well as dynamic light scattering (DLS). The fluorescence of BSA was strongly quenched by the binding of pegylated Pur to BSA. The binding constants and the number of binding sites of mPEG(5000)-Pur with BSA were 2.67±0.12 and 1.37±0.05 folds larger after pegylating, which were calculated from the data obtained from fluorescence quenching experiments. The enthalpy change (ΔH) and entropy change (ΔS) were calculated to be 4.09 kJ mol(-1) and 20.01 J mol(-1) K(-1), respectively, according to Van't Hoff equation, indicating that the hydrophobic force plays a main role in the binding interaction between pegylated Pur and BSA. In addition, the negative sign for Gibbs free energy change (ΔG) implies that the interaction process is spontaneous. Moreover, the results of synchronous fluorescence and CD spectra demonstrated that the microenvironment and the secondary conformation of BSA were changed. Comparing with Pur, all our data collected indicated that pegylated Pur interacted with BSA in the same way as that of Pur, but docked into the hydrophobic pocket of BSA with more accessibility and stronger binding force. DLS measurements showed monomethoxy polyethylene glycol (mPEG) have an effect on BSA conformation, and revealed that changes in BSA size might be due to increases in binding constant and the absolute values of ΔG after Pur pegylation.  相似文献   

13.
用荧光光谱法研究了在生理条件下,3-对氯苯基-2-(4-叔丁基苯氧基)-3’-氧环己烷并噻吩并[2,3-d]嘧啶-4(3H)-酮(PTP)与牛血清白蛋白(BSA)的相互作用。实验表明,PTP主要以静态猝灭方式使BSA荧光强度显著降低。计算了不同温度下二者的结合常数和结合位点数,并根据热力学参数确定了PTP与BSA之间的作用力主要为氢键或范德华力。根据Frster非辐射能量转移机理,测定了PTP与BSA相互结合时的作用距离,并用同步荧光技术讨论了其衍生物对BSA构象的影响。  相似文献   

14.
The interaction between azathioprine (AZ) and bovine serum albumin (BSA) is mainly due to hydrophobic binding according to the dependence of the binding constant on the ionic strength obtained by equilibrium dialysis. The binding constant and partition coefficient of AZ were smaller than those of warfarin, phenylbutazone and ibuprofen. Little variation in the proton chemical shift of AZ was observed whether there was an absence or presence of BSA (7.25 x 10(-5) M). The spin-lattice relaxation time (T1) of AZ decreased in the presence of BSA to 6-22%. The spin-spin relaxation rate (1/T2) of AZ increased 16-24 times for the methyl group and the imidazole ring and 8-13 times for the purine ring in the presence of BSA. The ratio of the spin-spin relaxation rate of the free AZ to the bound AZ ((1/T2)b/(1/T2)f) of the methyl group and the imidazole ring was 2-3 times larger than that of the purine ring. The binding of AZ to BSA was concluded to be mainly at the methyl group on the imidazole ring of AZ.  相似文献   

15.
Yang G  Zhao Y  Li M  Zhu Z  Zhuang Q 《Talanta》2008,75(1):222-226
The chiral resolution of three beta-blockers including propranolol, pindolol and oxprenolol, was studied by affinity electrokinetic chromatography. The effect of various chiral selectors and some key parameters including buffer pH, buffer concentration, capillary temperature and applied voltage were carefully studied, respectively. At optimum condition, based on the signal-to-noise ratio of 3, the detection limits for the simple resolution and chiral resolution were found to be 1.0x10(-5) and 4.0 x 10(-5)M, respectively. In addition, the interactions of these beta-blockers with bovine serum albumin (BSA) were studied and the binding constant (K(a)) between BSA and each of beta-blockers were calculated. Based on linear correlation coefficient, it can be concluded that the binding ratio of pindolol (oxprenolol) combining with BSA is 1:1, and that the binding number of propranolol interacting with BSA deviates one.  相似文献   

16.
The effect of heavy metal ions, Cd(2+), Hg(2+) and Pb(2+) on (+)-catechin binding to bovine serum albumin (BSA) has been investigated by spectroscopic methods. The results indicated that the presence of heavy metal ions significantly affected the binding modes and binding affinities of (+)-catechin to BSA, and the effects depend on the types of heavy metal ion. One binding mode was found for (+)-catechin with and without Cd(2+), while two binding modes - a weaker one at low concentration and a stronger one at high concentration were found for (+)-catechin in the presence of Hg(2+) and Pb(2+). The presence of Cd(2+) decreased the binding affinities of (+)-catechin for BSA by 20.5%. The presence of Hg(2+) and Pb(2+) decreased the binding affinity of (+)-catechin for BSA by 8.9% and 26.7% in lower concentration, respectively, and increased the binding affinity of (+)-catechin for BSA by 5.2% and 9.2% in higher concentration, respectively. The changed binding affinity and binding distance of (+)-catechin for BSA in the presence of Cd(2+), Hg(2+) and Pb(2+) were mainly because of the conformational change of BSA induced by heavy metal ions. However, the quenching mechanism for (+)-catechin to BSA was based on static quenching combined with non-radiative energy transfer irrespective of the absence or presence of heavy metal ions.  相似文献   

17.
Xiao J  Zhao Y  Mao F  Liu J  Wu M  Yu X 《The Analyst》2012,137(1):195-201
The effect of a ZnO#ZnS QDs heterojunction (O#SQDs) on the binding affinities of flavonoid glycosides for bovine serum albumin (BSA) was investigated. The fluorescence intensities of BSA decreased remarkably with increasing concentration of O#SQDs. The magnitudes of the binding constants of flavonoid glycosides for BSA in the presence of O#SQDs were in the range of 10(5)-10(7) L mol(-1), and the number of binding sites per BSA (n) was determined as 1.24 ± 0.17. O#SQDs increased the affinities of flavonoid glycosides for BSA by about 2.96% to 114.68% depending on their structures. O#SQDs in blood will enhance the transportation of flavonoid glycosidegs in blood and improve their pharmacology effects. From this point, O#SQDs are a perfect candidate for flavonoid glycosides delivery applications.  相似文献   

18.
The mechanism of interaction of vinblastin sulphate (VBS) with bovine serum albumin (BSA) has been reported. Association constant for VBS-BSA binding was found to be 3.146+/-0.06 x 10(4) M(-1). Stern-Volmer analysis of fluorescence quenching data showed that the fraction of fluorophore (protein) accessible to the quencher (drug) was close to unity indicating thereby that both tryptophan residues of BSA are involved in drug-protein interaction. The rate constant for quenching, greater than 10(10) M(-1) S(-1), indicated that the drug-binding site is in close proximity to tryptophan residues of BSA. Binding studies in the presence of an hydrophobic probe, 8-anilino-1-naphthalein-sulphonic acid, sodium salt (ANS) indicated that there is hydrophobic interaction between VBS and probe and they do not share common sites in BSA. Thermodynamic parameters obtained from data at different temperatures showed that the binding of VBS to BSA involves predominant hydrophobic forces. The effects of some additives and paracetamol on binding of VBS-BSA have also been investigated. The CD spectrum of BSA in presence of VBS shows that the binding of VBS leads to change in the helicity of BSA.  相似文献   

19.
With the fluorescence probe of 8-anilino-1-naphthalenesulfonate (ANS), the binding modes of terminally substituted alkane analogues (C(n)X; X = COOH, OH, CHO, NH(3), CONH(2)) to bovine serum albumin (BSA) were investigated using a competitive binding technique. The Scatchard plot of the fluorometric titration of BSA with ANS showed that the maximum binding number of ANS, n(max), was 3.81, with the binding constant, K(bnd), of 1.42 x 10(6) mol(-1) dm(3). The binding modes of C(n)X to BSA were analyzed based on the fluorometric titration of the ANS and BSA mixture with C(n)X. C(n)COOH completely displaced the ANS bound to BSA, whereas C(n)OH and C(n)CHO displaced only about 40% of the ANS bound to BSA. In contrast, C(n)NH(2) and C(n)CONH(2) displaced very little bound ANS. By comparing these results, we classified the binding modes of C(n)X to BSA into three types. Two of them are detectable with the ANS fluorescence and the remaining one is not detectable with the fluorescence.  相似文献   

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