Determination of proteins by fluorescence quenching of erythrosin B

Qi, Chun; Li, Ke An; Shen, Tong

doi:10.1016/0003-2670(96)00280-2

Cited by 57 publications

(21 citation statements)

References 10 publications

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“…The qualitative and quantitative analysis of proteins, especially the microdetermination of proteins, is one of the basic requisites in biochemical assays and clinical tests. Many methods have been proposed for the study of the binding reaction with protein such as spectrophotometry [1][2][3], fluorometry [4][5][6] and light scattering techniques [7][8][9][10]. The traditional methods are the Bradford method [11], the Lowry method [12] and bromocresol purple technique [13].…”

Section: Introductionmentioning

confidence: 99%

Electrochemical studies of the reaction between albumin and amaranth and its analytical application

Sun

Jiao

Wang

et al. 2005

Journal of Electroanalytical Chemistry

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Section: Introductionmentioning

confidence: 99%

Electrochemical studies of the reaction between albumin and amaranth and its analytical application

Sun

Jiao

Wang

et al. 2005

Journal of Electroanalytical Chemistry

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“…Protein can be stained by means of both hydrophobic interaction between aromatic rings of EY and hydrophobic sites of the protein and by the electrostatic interaction between anionic carboxylic and phenolic groups of EY and the certain residues of protein [19][20][21][22][23]. Therefore, successful use of this dye depends on the development of staining procedures where to enhance hydrophobic interactions and electrostatic binding between EY and proteins.…”

Section: Introductionmentioning

confidence: 99%

High‐throughput negative detection of SDS‐PAGE separated proteins and its application for proteomics

et al. 2010

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A negative detection method for proteins on SDS-PAGE is described. In this method, Eosin Y (EY) was selectively precipitated in the gel background, which is absent from those zones where proteins are located through the formation of a stable water-soluble protein-dye complex. Negative staining of proteins using EY, allows high-sensitivity, lowcost, and simple protocol. The new described method takes less than an hour to complete all the protocol, with a detection limit of 0.5 ng of single protein band. Comparing with imidazole-zinc negative stain, EY dye provides broader linear dynamic range, higher sensitivity and reproducibility, and better obvious contrast between the protein bands or spots and background. Furthermore, the novel technique developed here presented a real practical method for simultaneous processing of multiple gels, which makes it possible to perform high-throughput staining for proteome research. Additionally, we have also compared the influence of staining method on the quality of mass spectra by PMF.

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“…The quantitation of proteins is also a basic requisite in bioanalytical chemistry and clinical test. Nowadays many analytical methods such as spectrophotometry [8,9], fluorometry [10,11] and light scattering technique [12,13] have been proposed for the protein assay. For example the Bradford method is commonly used in clinical laboratories by using Coomassie brilliant blue G-250 (CBB G-250) and measuring the increase of absorbance value at 595 nm [14].…”

Section: Introductionmentioning

confidence: 99%

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

2010

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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 BrittonRobinson (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 À 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 (b s ) and the binding number (m) of HSA with [Cup-Cd(II)] complex were calculated by the voltammetric data with the results as b s ¼ 1.12 Â 10 6 and m ¼ 1.

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Determination of proteins by fluorescence quenching of erythrosin B

Cited by 57 publications

References 10 publications

Electrochemical studies of the reaction between albumin and amaranth and its analytical application

Electrochemical studies of the reaction between albumin and amaranth and its analytical application

High‐throughput negative detection of SDS‐PAGE separated proteins and its application for proteomics

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

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