阻抑动力学光度法测定食物中痕量草酸

水果;蔬菜;溴甲酚紫;阻抑动力学光度法测定食物中痕量草酸     

高碘酸钾氧化溴甲酚紫动力学光度法测定间苯二酚

在碱性和沸水浴条件下,微量的间苯二酚对高碘酸钾氧化溴甲酚紫褪色的反应具有显著的促进作用,据此建立了测定间苯二酚的新动力学光度法。该方法测定间苯二酚的线性范围为0．10～5．0μg／mL,检出限为0．041μg／mL,对于2．0μg／mL的间苯二酚11次测定的相对标准偏差是1．94％。方法用于皮炎宁酊及水样中间苯二酚的测定,结果满意。     

饮用水中二氧化氯的溴甲酚紫光度测定法

1　引　　言二氧化氯是很好的饮用水消毒杀菌剂。美国环保局建议ＣｌＯ2 处理饮用水的浓度不高于 1ｍｇ ｌ。测定水中ＣｌＯ2 的方法有多种 ,但快速、简便的方法不多见。本文研究了酸性溶液中 ,ＣｌＯ2 对溴甲酚紫的氧化褪色作用 ,建立了用溴甲酚紫测定水中微量ＣｌＯ2 的分光光度法 ,其线性范围 0～ 2 .8ｍｇ Ｌ,检出限 0 .0 1ｍｇ Ｌ ,相关系数ｒ=0 .995 8,用于水样分析 ,结果令人满意。2　实验部分2 1　仪器与试剂　 72 2型分光光度计 (上海分析仪器厂 ) ;ＣｌＯ2 标准溶液 6ｍｇ Ｌ ,避光于 0℃温度下保存 ;0 .1 1 5ｍｍｏｌ Ｌ溴甲酚…     

溴甲酚紫的极谱研究

溴甲酚紫是一应用广泛的有机式剂^[1-4]。关于羟基三苯甲烷类染料的极谱研究报导不多^[5]。Ghoneim^[6]曾报导溴甲酚紫在pH<7时产生一个2电子还原波,当pH大于10时,可产生两个1电子还原波。Goel^[7]只研究了第一波的还原机理。本文用普通极谱、脉冲极谱、循环伏安等方法较详细地研究了溴甲酚紫的电还原。提出一电还原机理,解释了半波电位随pH变化的特殊规律。     

原子吸收法间接测定Mo—Fe—S原子簇化合物中的硫

关于Mo-Fe-S原子簇化合物中硫的测定已经有些报道。为了同其中的钼铁含量的测定相配合,这里报道一种通过铬含量的原子吸收测定,而间接测定硫的方法。准确称取待测样品5—7mg,置于小烧杯中,加入1ml浓硝酸,盖上表面皿,氧化一会,再放到电炉上加热,使样品充分消解氧化,待溶液呈淡黄透明状取下(不能蒸干)。冷后加入少许水,滴入一滴0.2％的溴甲酚紫指示剂,再     

某些酸性三苯甲烷染料与盐酸吡格列酮相互作用的分子光谱特点及其分析应用

溴甲酚绿;氯酚红;酚红;溴甲酚紫;盐酸吡格列酮;分光光度法     

催化光度法测定痕量钒——钒（V）-溴甲酚紫-过氧化氢体系

催化光度法测定钒已有报道[1~3],在0.45 mol·L-1磷酸介质及加热条件下,过氧化氢氧化溴甲酚紫褪色反应非常缓慢,而痕量钒对此反应具有较高的催化活性,且在一定浓度范围内,钒量与褪色反应程度呈线性关系,据此可建立测定痕量钒的方法。方法的检出限为1.9×10-6g·L-1,测定范围为0·003~1.8 mg·L-1。方法操作简便,重现性好,用于钢样中痕量钒的测定,结果满意。1试验部分1.1仪器与试剂721型分光光度计LB801-2型超级恒温器钒(Ⅴ)标准溶液:1.000 0 g·L-1,称取偏钒酸铵0.229 7 g溶于热水中,冷却,定容于100 mL容量瓶中。溴甲酚紫(用R表示)溶液:…     

催化光度法测定痕量甲醛

基于磷酸介质中甲醛催化溴酸钾氧化溴甲酚紫的褪色反应 ,建立了测定痕量甲醛的方法。方法的检出限为 1.0× 10 - 5g·L- 1,线性范围为 0 .0 2 0～ 0 .4 8μg·ml- 1,方法简便 ,用于空气中测定痕量甲醛 ,结果满意。     

痕量铈的催化动力学光度法测定

基于pH 9．0的氨水-氯化铵缓冲溶液中,痕量铈(Ⅳ)对溴酸钾氧化溴甲酚紫褪色的指示反应有明显的催化作用。据此建立了痕量铈(IV)的光度测定法,铈量在0～4．0μg·L-1间与△A值间呈线性关系,检出限为0．092μg·L-1。用于测定人发、茶叶和大米样品中痕量铈(IV),结果的相对标准偏差在3．6％～5．4％之间,回收率在96％～103％之间。     

痕量铜(Ⅱ)的催化光度法测定——铜(Ⅱ)-溴甲酚紫-过氧化氢体系

1 引言 在稀氨水介质中,痕量铜(Ⅱ)对H_2O_2氧化溴甲酚紫的反应有强烈的催化作用。本文利用该催化体系,建立了痕量铜(Ⅱ)的催化光度分析的新方法。该方法不仅灵敏度高,选择性好,而且操作简便,易于推广应用。 2 实验方法 采用固定时间法。选用刻度一致的两支具玻塞的25ml比色管,分别加入0.5ml溴甲酚紫,1.5ml氨水     

Studies on the interaction of protein with acid chrome blue K by electrochemical method and its analytical application

An electrochemical investigation on the interaction of acid chrome blue K (ACBK) with protein on the mercury electrode with different electrochemical methods such as cyclic voltammetry and linear sweep voltammetry was reported in this paper. In pH 3.0 Britton-Robinson (B-R) buffer solution, ACBK has an irreversible voltammetric reductive peak at -0.23 V (vs. SCE). The addition of human serum albumin (HSA) into the ACBK solution resulted in the decrease of reductive peak currents without the change of the peak potential and no new peaks appeared on the cyclic voltammogram. In the absence and presence of HSA, the electrochemical parameters such as the formal potential E0, the electrode reaction standard rate constant k(s) and the charge transfer coefficient alpha of the interaction system were calculated and the results showed that there were no significant changes between each other. Thus, the interaction of ACBK with protein forms an electro-inactive supramolecular bio-complex, which induces the decrease of the free concentration of ACBK in the reaction solution, and the decrease of the reductive peak current of ACBK. The binding constant and the binding ratio are calculated as 1.29 x 10(8) and 1:2, respectively, and the interaction mechanism is discussed. Based on the binding reaction, this new electrochemical method is further applied to the determination of HSA with the linear range from 3.0-20.0 mg/L and the linear regression equation as deltaIp"(nA) = 10.08 + 19.90 C (mg/L). This method was further applied to determinate the content of protein in the healthy human serum samples with the results in good agreement with the traditional Coomassie brilliant blue G-250 spectrophotometric method.     

A New Electrochemical Method for the Determination of Proteins with Cupferron‐Cadmium(II) Complex

A new electrochemical method was proposed for the determination of trace amounts of proteins based on the cupferron (Cup) and cadmium(II) complex [Cup‐Cd(II)] as the voltammetric probe. In the selected pH 6.5 Britton–Robinson (B–R) buffer solution, Cup can interact with Cd(II) to form a stable complex of [Cup‐Cd(II)], which had a sensitive linear sweep voltammetric reductive peak at ?0.654 V (vs. SCE). The addition of human serum albumin (HSA) into [Cup‐Cd(II)] complex solution could greatly decrease the reductive peak current without the change of the reductive peak potential, which indicated that HSA could interact with [Cup‐Cd(II)] complex to form a supramolecular biocomplex. The interaction mechanism was discussed and the decrease of reductive peak current was proportional to the concentration of HSA, which could be further used for the proteins determination. The optimal conditions of the binding reaction and the electrochemical detection were carefully investigated. Under the optimal conditions a new quantitative determination method for different kinds of proteins such as HSA, bovine serum albumin (BSA) and bovine hemoglobin (BHb) etc. was developed. The proposed method was simple, practical and relatively free from the interferences of coexisting substances, and it was further applied to the samples determination with satisfactory results. The binding constant (β_s) and the binding number (m) of HSA with [Cup‐Cd(II)] complex were calculated by the voltammetric data with the results as β_s=1.12×10⁶ and m=1.     

Linear sweep voltammetric determination of protein based on its interaction with Alizarin Red S

In this paper, the electrochemical behavior of the interaction of Alizarin Red S (ARS) with bovine serum albumin (BSA) was investigated on the hanging mercury drop electrode (HMDE). In the acidic solution (pH 4.2), ARS can be easily reduced on the HMDE and it has a well-defined polarographic wave at −0.29 V (SCE). On addition of BSA or human serum albumin (HAS) into the ARS solution, the reduction peak current of ARS decreases without the movement of the peak potential and the appearance of new peaks. The study shows that a new electrochemically non-active complex is formed via intercalation of ARS with BSA or HSA, which can not be reduced on the Hg electrode. The decrease of reductive peak current of ARS is proportional to BSA and HSA concentration in the range of 2.0–60 and 2.0–40 mg l⁻¹, respectively. The detection limit of BSA and HSA is 1.0-mg l⁻¹. The analytical results of human serum and urine samples by this method were in good agreement with the Coomassie brilliant blue G-250 assay. The binding number and the binding interaction mechanism are also discussed.     

Voltammetric Studies on Chromotrope 2B‐Protein Interaction and Its Analytical Application

In this paper the interaction of chromotrope 2B (Ch2B) with proteins was studied by the electrochemical method. Ch2B is an azo dye and shows irreversible electrochemical responses on the mercury electrode in a pH 3.0 Britton‐Robinson (B‐R) buffer solution. After the addition of human serum albumin (HSA) into the Ch2B solution, an interaction took place, and a supramolecular complex was formed in the mixed solution. The electrochemical parameters of the Ch2B‐HSA interaction system were calculated and compared. The results showed that in the absence and presence of HSA in Ch2B solution, the electrochemical parameters such as the formal potential E⁰, the electrode reaction standard rate constant k_s, etc. showed no significant changes, which indicated that an electro‐inactive supramolecular biocomplex was formed. The free concentration of Ch2B in reaction solution was decreased, and this resulted in the decrease of the peak current. The binding constant and the binding ratio were calculated as 7.85 × 10⁹ and 1:2, respectively, and the interaction mechanism was discussed. Based on the decrease of the peak current, this new electrochemical method was proposed for the determination of HSA in the concentration range of 2.0?25.0 mg/L with the linear regression equation as ΔIp′ (nA) = 50.56C (mg/L) — 6.72 (γ = 0.995). This method was further used to determine other different kinds of proteins, such as bovine serum albumin (BSA), oval albumin, etc‥ The new method was successfully applied to detect the content of albumin in healthy human serum samples with the results in good agreement with the traditional Coomassie Brilliant Blue G‐250 spectrophotometric method.     

Application of arsenazo III for the polarographic detection of proteins

In this paper, a diazo dye of arsenazo III (AAIII) was selected as a new electrochemical probe for the determination of proteins. In Britton-Robinson (B-R) buffer solution of pH 2.4, AAIII had a sensitive second order derivative linear sweep voltammetric reductive peak at ?0.39 V (vs. SCE). After the addition of human serum albumin (HSA) into AAIII solution, an interaction was taken place in the mixed solution and a biosupramolecular complex was formed, which resulted in the decreased reductive peak currents of AAIII. Based on the observed decrease in peak current, a sensitive electrochemical method was proposed for the determination of different proteins such as HSA, bovine serum albumin (BSA) and bovine hemoglobin (BHb). The optimal conditions for the interaction and the interfering effects of coexisting substances on the detection were investigated. The proposed method was successfully applied to the determination of HSA in synthetic samples with the recoveries in the range of 99.13–100.50%. The stoichiometry of HSA-AAIII biocomplex was calculated by voltammetric data with a binding number of 2 and a binding constant of 7.53 × 10⁹.     

Studies on the Interaction of Beryllon Ш with Proteins by Voltammetric Technique and its Application

A new quantitative determination method of proteins using beryllon Ш by voltammetric technique was developed in this paper. In pH 3.5 Britton-Robinson (B-R) buffer solution, beryllon Ш can bind with human serum albumin (HSA) to form an electro-inactive supermolecular complex. Beryllon Ш has a well-defined voltammetric reduction peak at -0.38 V (vs. SCE) and the addition of protein in this solution can cause the decrease of the reductive peak current. Based on the decrease of the reduction peak current, a new electrochemical method for the determination of HSA was established with linear range of 1.0~40.0 mg/L and the detection limit of 1.0 mg/L. This method is further applied to the determination of real sample of healthy human serum.     

Studies on the Interaction of Beryllon Ⅲ with Proteins by Voltammetric Technique and its Application

A new quantitative determination method of proteins using beryllon Ⅲ by voltammetric technique was developed in this paper. In pH 3.5 Britton-Robinson (B-R) buffer solution, beryllon Ⅲ can bind with human serum albumin (HSA) to form an electro-inactive supermolecular complex. Beryllon Ⅲ has a well-defined voltammetric reduction peak at -0.38 V (vs. SCE) and the addition of protein in this solution can cause the decrease of the reductive peak current. Based on the decrease of the reduction peak current, a new electrochemical method for the determination of HSA was established with linear range of 1.0-40.0 mg/L and the detection limit of 1.0 mg/L. This method is further applied to the determination of real sample of healthy human serum.     

偶氮氯膦Ⅲ与人血清白蛋白相互作用的电化学研究

偶氮氯膦Ⅲ是一种具有电化学活性的染料,在pH3.5的Britton-Robinson缓冲溶液中,它可以与人血清白蛋白发生相互作用形成一种生物超分子复合物,使溶液中游离的染料浓度降低.以线性扫描二阶导数极谱法对偶氮氯膦Ⅲ-人血清白蛋白的相互作用体系进行了详细的研究,复合物的形成使偶氮氯膦Ⅲ在-0.124V(vs.SCE)的还原峰电流降低,考察了结合反应的最佳条件和测定条件,求解了结合常数和结合比.     

Electrochemical Study on the Interaction of Protein with Bromothymol Blue and Its Analytical Application

The interaction of bromothymol blue（BB） with human serum albumin（HSA） was studied by electrochemical techniques and a sensitive method for proteins assay was developed. When BB interacted with HSA, the voltammetric peak current value of BB decreased linearly with the concentration of HSA in a range of 1.0--40.0 mg/L, and the peak potential shifted negatively. Based on the results, a sensitive assay method for proteins, such as HSA, bovine serum albumin（BSA）, and egg albumin etc. was established. This method was further applied to determining the HSA in healthy human blood samples, and the results are not significantly different from those obtained by the classic Coomassie Brilliant Blue G-250 spectrophotometic method. The detecting conditions of this method were optimized and the interaction mechanism was discussed. The results show that the electrochemical parameters（formal potential E^0, standard rate constant of the electrode reaction ks, parameter of kinetic nα） of BB have no obvious changes before and after the interaction, which indicate that BB can interact with HSA, forming an electrochemical non-active complex. The equilibrium constant（βs） and the binding ratio（m） for this complex were calculated. The m is 4 and βs is 1.41 × 10^19. This method is fast, simple, highly sensitive, and has good selectivity, which can be used in clinical measurements.     

Application of Cupferron‐lead(II) Complex for the Electrochemical Determination of dsDNA

Based on the interaction of cupferron and lead(II) complex [Cup‐Pb(II)] with double‐stranded DNA (dsDNA) a new voltammetric method for the detection of DNA was described in this paper. In pH 4.0 HAc‐hexamine buffer solution, [Cup‐Pb(II)] complex showed a sensitive second order derivative polarographic reductive peak at ‐0.554 V (vs. SCE). After the addition of dsDNA into [Cup‐Pb(II)] mixture solution the reductive peak current decreased with the positive shift of reductive peak potential, which was the typical characteristic of intercalation mode. Under the optimum conditions, the decrease of reductive peak current was directly proportional to the dsDNA concentration in the range from 1.0 to 25.0 mg/L with the linear regression equation as ΔIp″ (nA) = 129.30 + 62.51 C (mg/L) (n = 13, γ = 0.991). The detection limit of 0.90 mg/L (3σ) and the relative standard derivation (RSD) of 2.43% for 10 parallel determinations of 10.0 mg/L dsDNA were found. The method was successfully applied to synthetic samples with good results, and the stoichiometry of dsDNA with [Cup‐Pb(II)] complex was calculated by the voltammetic data with the binding number as 2 and the binding constant as 2.82 × 10⁹.