共查询到18条相似文献,搜索用时 62 毫秒
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伊红Y分光光度法测定血清白蛋白 总被引:8,自引:0,他引:8
在 p H 3.2 9缓冲介质中 ,牛血清白蛋白与伊红 Y结合 ,形成 EY- BSA复合物 ,以试剂空白参比 ,在 5 4 5 nm处产生一灵敏的吸收峰 ,BSA的浓度在 0~ 1 .6×1 0 - 7mol/L范围内与 5 4 5 nm处的吸光度呈良好的线性关系 ,摩尔吸光系数 ε=2 .1 2× 1 0 6 L· mol- 1· cm- 1,Sandell灵敏度为 0 .0 32 μg/cm2 ,方法对 BSA的检出限为9.2× 1 0 - 9mol/L。本法具有灵敏度高、选择性好等特点 ,用于人血清样品中蛋白质的测定 ,与经典的考马斯亮蓝 G- 2 5 0方法结果一致 相似文献
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双波长K系数分光光度法测定血清钙 总被引:4,自引:0,他引:4
提出了一种新的用于单组分测定的双波长分光光度测定方法,以显色剂的最大吸收波长作参比波长,以显色络合物的最大吸收波工为测定波长,采用不加显色剂的试剂空白作参比,用K-系数法在同一分析体系中消除过量显色剂的干扰。理论实验表明,该方法可显著地提高光度法的灵敏度和精密度,尤其对测定波长处显色剂干扰较大的体系效果更为明业,利用该方法测定了血清Ca^2+结果满意。 相似文献
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溴甲酚绿分光光度法测定牛血清白蛋白 总被引:2,自引:0,他引:2
在pH 3.3的Britton-Robinson (B-R)缓冲溶液中, 对溴甲酚绿(BCG)与牛血清白蛋白(BSA)相互作用的吸收光谱进行了初步研究. 结果表明: BCG与BSA作用在室温下能迅速结合成复合物, 并且随着BSA的浓度增大, 在444 nm处的吸收峰降低, 618 nm处吸收峰升高并红移至628 nm. 在此波长下测定其复合物的吸光度, 其吸光度的增加值(ΔA)与BSA的质量浓度在8~260 μg/mL范围内呈良好的线性关系(r=0.9996), 检出限为4 μg/mL. 该方法应用于鲜奶粉和液态纯牛奶样品中总蛋白的测定, 回收率分别为92.7%, 95.5%, 结果与考马斯亮蓝G250法基本一致. 相似文献
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在pH 4.6的HAc-NaAc缓冲溶液中,对橙皮苷与牛血清白蛋白(BSA)相互作用的吸收光谱进行了初步研究.结果表明,橙皮苷在236 nm处有一强的吸收峰,当加入BSA作用后该吸收峰的强度升高,峰位基本不变,且没有新的吸收峰出现.在此波长下测定其复合物的吸光度,其吸光度的增加值(ΔA)与BSA的浓度在16~260 μg/mL范围内呈良好的线性关系(r=0.999 3),检出限为10 μg/mL,测定结果的相对标准偏差为3.2%(n=10).该方法具有简便、快速、选择性好、灵敏度高等特点,应用于鲜奶粉和液态纯牛奶样品中总蛋白的测定,回收率分别为87.5%、92.4%,结果与考马斯亮蓝G250法基本一致. 相似文献
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酸性棕NR分光光度法测定血清白蛋白 总被引:3,自引:1,他引:2
采用分光光度法研究了酸性棕NR与血清白蛋白的结合反应。在Brit ton Robinson(B-R)(pH2.50)缓冲溶液中,酸性棕NR与血清白蛋白结合生成沉淀,探讨了该结合反应的最佳条件,并据此建立了一种高灵敏度的测定血清白蛋白的新方法。牛血清白蛋白(BSA)和人血清白蛋白(HSA)分别在28.0~112.0mg/L、24.4~122.0mg/L范围内服从比尔定律,其表观摩尔吸光系数分别为:1 44×106L·mol-1·cm-1(BSA)、1.32×106L·mol-1·cm-1(HSA)。对7个人血清样品蛋白总量平行测定6次,相对标准偏差0.83%~3.02%,回收率90.90%~109.80%,且与医院双缩脲法结果基本一致。 相似文献
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分光光度法同时测定人发中的钙,锌 总被引:1,自引:0,他引:1
将多元线性回归分析用于分光光度法同时测定人发中钙,锌元素的含量,讨论了该方法的原理,考察了最佳实验条件,建立了回归方程和线性方程。对6人模拟发样和2个人发样品进行了测定,结果令人满意。 相似文献
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A new spectrofluorimetric method is proposed for determination of human serum albumin (HSA) with the limit of detection at ng levels. Using doxycycline (DC)-europium (Eu3+) as a fluorescent probe, in a buffer solution of pH 10.2, HSA can remarkably enhance the fluorescence intensity of the DC-Eu3+ complex at 612 nm and the enhanced fluorescence intensity of Eu3+ is proportional to the concentration of HSA. Optimum conditions for the determination of HSA are also investigated. The linear ranges for HSA are 0-9.2 and 9.2-34.5 μg ml−1 with limits of detection of 64 and 115 ng ml−1, respectively. This method is simple, practical and relatively free of interference from coexisting substances, as well as much more sensitive than most of the existing assays. The determination results for human serum and urine samples are identical to those by the AOAO method, with relative standard deviations of five determinations of 1.1-3.6%. By the Rosenthal graphic method, the binding number and association constant of human serum albumin with the probe are 1.8 and 3.71×105 l mol−1, respectively. 相似文献
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Cheng FQ Wang YP Li ZP Dong C 《Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy》2006,65(5):1144-1147
The binding of bromsulphalein (BSP) with human serum albumin was investigated at different temperatures, 298 and 308 K, by the fluorescence spectroscopy at pH 7.24. The binding constant was determined by Stern-Volmer equation based on the quenching of the fluorescence HSA in the presence of bromsulphalein. The effect of various metal ions on the binding constants of BSP with HSA was investigated. The thermodynamic parameters were calculated according to the dependence of enthalpy change on the temperature as follows: DeltaH and DeltaS possess small negative (9.3 kJ mol(-1)) and positive values (22.3 J K(-l)mol(-l)), respectively. The experimental results revealed that BSP has a strong ability to quench the intrinsic fluorescence of HSA through a static quenching procedure. The binding constants between BSP to HSA were remarkable and independent on temperature. The binding constants between HSA and BSP decreased in the presence of various ions, commonly decreased by 30-55%. The hydrophobic force played a major role in the interaction of BSP with HSA. All these experimental results and theoretical data clarified that BSP could bind to HSA and be effectively transported and eliminated in body, which could be a useful guideline for further drug design. 相似文献
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de la Escosura-Muñiz A González-García MB Costa-García A 《Analytical and bioanalytical chemistry》2006,384(3):742-750
A new electroactive label has been used to monitor immunoassays in the determination of human serum albumin (HSA) using glassy-carbon
electrodes as supports for the immunological reactions. The label was a gold(I) complex, sodium aurothiomalate, which was
bound to rabbit IgG anti-human serum albumin (anti-HSA-Au). The HSA was adsorbed on the electrode surface and the immunological
reaction with gold-labelled anti-HSA was then performed for one hour by non-competitive or competitive procedures. The gold(I)
bound to the anti-HSA was electrodeposited in 0.1 mol L−1 HCl at −1.00 V for 5 min then oxidised in 0.1 mol L−1 H2SO4 solution at +1.40 V for 1 min. Silver electrodeposition at −0.14 V for 1 min followed by anodic stripping voltammetry were
then performed in aqueous 1.0 mol L−1 NH3–2.0×10−4 mol L−1 AgNO3. For both non-competitive and competitive formats, calibration plots in the ranges 5.0×10−10 to 1.0×10−8 mol L−1 and 1.0×10−10 to 1.0×10−9 mol L−1 HSA, respectively, with estimated detection limits of 1.5×10−10 mol L−1 (10 ng mL−1) and 1.0×10−10 mol L−1 (7 ng mL−1), respectively, were obtained. Levels of HSA in two healthy volunteer urine samples were also evaluated, using both immunoassay
formats. 相似文献
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Summary The interaction thermodynamics of heptacarboxylporphyrin (HCP) and protoporhyrin (PP) with human serum albumin (HSA) was studied
by affinity capillary electrophoresis (ACE) over the temperature range of 25–50°C, where HCP and PP bound to HSAvia 1:1 molecular association. The binding equilibrium constants (pH 7.4, phosphate buffer) for the binding of HCP with HSA were
found to decrease with an increase in temperature, whereas the binding constants of the PP/HSA system appeared to be independent
of temperature changes over the range studied. The van’t Hoff relationship (25–50°C) was found to be linear for the interaction
of either HCP or PP with HSA. However, the interaction thermodynamics for both of these porphyrins with HSA were found to
be quite different. In particular, the interaction of HCP (a hydrophilic porphyrin) with HSA appeared to be based on an enthalpy-driven
process, whereas the binding between PP (a hydrophobic porphyrin) and HSA driven by a favorable change in entropy. The ability
of using ACE to evaluate the interaction thermodynamics of serum proteins (e.g., HSA) with ligands (e.g., porphyrins and related
compounds) should aid in the development of new and more effective photosensitizers in the photodynamic therapy of cancer. 相似文献
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利用荧光及紫外光谱法研究了水溶液中洛美沙星(LMX)与人血清白蛋白(HSA)的相互作用机理. 结果表明洛美沙星对人血清白蛋白的荧光有较强的猝灭作用, 其猝灭类型主要为静态猝灭. 在不同温度下求得了洛美沙星与人血清白蛋白的结合常数K, 发现随反应温度上升K值下降. 由热力学参数确定了洛美沙星与人血清白蛋白的结合作用主要为色散力. 用同步荧光技术考察了洛美沙星对人血清白蛋白构象的影响, 又根据Fōrster理论, 测得了洛美沙星与人血清白蛋白之间的能量转移效率, 相互结合距离. 进一步证明了该反应是单一静态猝灭过程, 阐述了其猝灭机理是通过能量转移产生的. 相似文献
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Yan-Qing Wang Hong-Mei Zhang Gen-Cheng Zhang Wei-Hua Tao Shu-He Tang 《Journal of Molecular Structure》2007,830(1-3):40-45
The feature of brucine binding to human serum albumin (HSA) was investigated via fluorescence and UV/vis absorption spectroscopy. The results revealed that brucine caused the fluorescence quenching of HSA by the formation of brucine–HSA complex. The hydrophobic interaction plays a major role in stabilizing the complex; the binding site number n and apparent binding constant KA, corresponding thermodynamic parameters the free energy change (ΔG), enthalpy change (ΔH) and entropy change (ΔS) at different temperatures were calculated. The distance r between donor (HSA) and acceptor (brucine) was obtained according to fluorescence resonance energy transfer. The effect of brucine on the conformation of HSA was analyzed using synchronous fluorescence spectroscopy and UV/vis absorption spectroscopy. 相似文献