Microdetermination of proteins by Rayleigh light scattering technique with acid green 25

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

doi:10.1016/s0003-2670(96)00444-8

Analytica Chimica Acta

1997

DOI: 10.1016/s0003-2670(96)00444-8

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Microdetermination of proteins by Rayleigh light scattering technique with acid green 25

Chun Qi

Ke An Li

Tong Shen

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Cited by 63 publications

(18 citation statements)

References 10 publications

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“…[2][3][4][5][6][7][8] It has been proved that the enhanced RLS signals which resulted from the aggregation and assembly processes can be applied to highly sensitive quantifications of DNA, 9,11 proteins, [12][13][14] ions, 15 surfactants 16 and clinical medicines [17][18][19] by using a common spectrofluorometer. These measurements, however, depend on the measuring conditions, including the molecular absorption, instrument conditions, reflection and scattering of the inside and outside walls of the absorption cell.…”

mentioning

confidence: 99%

Determination of Proteins with Fast Red VR by a Corrected Resonance Light-Scattering Technique

Yang¹,

Li²,

Huang³

2003

ANAL. SCI.

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A simple corrected resonance light-scattering (CRLS) technique was established to correct for any distortion of the resonance light scattering (RLS) spectra resulting from molecular absorption. By using an absorption cell holder to change the propagation direction of the incident light beam of a common spectrofluorometer, the molecular absorption was directly measured through a spectrofluorometer. With measurements of the CRLS signals of the interaction of Fast Red VR (FRV) and proteins, we proved that the present correction for the RLS spectra in terms of the molecular absorption of excitation and scattering radiation can improve the detection sensitivity by about two fold.

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Determination of Proteins with Fast Red VR by a Corrected Resonance Light-Scattering Technique

Yang¹,

Li²,

Huang³

2003

ANAL. SCI.

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“…Under the optimal conditions the decrease of peak current was proportional to the concentration of protein and further used to the determination of different kinds of proteins. The calibration curves for the determination of HSA, bovine serum albumin (BSA), ovalbumin (OVA), bovine hemoglobin (BHb), lipase were linear over the ranges of 4.0~28.0 mg L [6][7][8][9] In this paper electrochemical method was applied to investigate the interaction of orange G with proteins. Compared with other often-used methods such as spectrophotometry, fluorometry and chemiluminicence, electrochemical method is seldom used in studying the protein binding reaction.…”

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confidence: 99%

Voltammetric studies on the interaction of orange G with proteins: analytical applications

Sun¹,

Han²,

Yong³

et al. 2006

J. Braz. Chem. Soc.

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A interação do alaranjado G com proteína foi investigada pela técnica de voltametria. O alaranjado G, em solução tampão Britton-Robinson (B-R), pH 2,0, mostrou um pico voltamétrico irreversível de redução, a -0,17V (vs. SCE) utilizando mercúrio como eletrodo de trabalho. A adição de albumina de soro humano (HSA) à solução de alaranjado G, resultou no decréscimo do pico de corrente de redução, aparentemente sem variações dos portenciais de pico e sem o surgimento de novos picos de corrente. Os parâmetros eletroquímicos da solução de alaranjado G, na ausência e presença de HSA, foram calculados e comparados. Os resultados mostraram que não ocorreram variações significantes, indicando que o comportamento eletroquímico da solução reacional utilizando mercúrio como eletrodo de trabalho não variou e que foi formado um biocomplexo supramolecular, eletroquimicamente inativo. O mecanismo de interação foi devido à formação do campo microeletrostático na estrutura da albumina em solução aquosa, causando a interação com o alaranjado G, o que induziu o decréscimo da concentração de equilíbrio do alaranjado G na solução reacional, e o decréscimo do pico de corrente de redução. As condições de interação foram discutidas cuidadosamente. Sob condições ótimas, o decréscimo do pico de corrente foi proporcional à concentração da proteína e posteriormente, usado para a determinação de diferentes tipos de proteínas. As curvas de calibração para a determinação de HSA, albumina de soro bovino (BSA), ovalbumina (OVA), hemoglobina bovina (BHb) e lipase, foram lineares nos intervalos de 4,0~28,0 mg L The interaction of orange G with protein was investigated by voltammetric method in this paper. In pH 2.0 Britton-Robinson (B-R) buffer solution orange G displayed an irreversible voltammetric reduction peak at -0.17 V (vs. SCE) on mercury working electrode. The addition of human serum albumin (HSA) into the orange G solution resulted in the decrease of the reduction current peak apparently without the changes of peak potentials and no new peaks appeared. The electrochemical parameters of orange G solution in the absence and presence of HSA were calculated and compared. The results showed that there were no significant changes, which indicated that the electrochemical behaviors of reaction solution on the mercury working electrode showed no changes and a supramolecular electrochemical inactive biocomplex was formed. The interaction mechanism was due to the formation of the microelectrostatic field in albumin structure in aqueous solution and caused the interaction with orange G, which induced the decrease of the equilibrium concentration of orange G in the reaction solution, and the decrease of the reductive peak current. The interaction conditions were discussed carefully. Under the optimal conditions the decrease of peak current was proportional to the concentration of protein and further used to the determination of different kinds of proteins. The calibration curves for the determination of HSA, bovine serum albumin (BSA), ovalbumin (OVA)...

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“…Ma et al (9)(10)(11) used this technique for protein assay, and subsequently this method has attracted the attention of many researchers (12)(13)(14)(15).…”

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confidence: 99%

Resonance light scattering technique for the determination of proteins with Congo red and Triton X‐100

Sun

Guo

et al. 2005

Luminescence

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Resonance light scattering (RLS) of Congo red (CR) was greatly enhanced by BSA (HSA) in the presence of Triton X-100 (TX-100). In sodium citrate-HCl buffer (pH 2.7-3.0), the enhanced intensity of resonance light scattering at 360 nm was in proportion to the concentration of proteins [corrected] The linear relationship was obtained between the resonance light scattering intensity and proteins in the range 5.0 x 10(-8)-8.0 x 10(-6) g/mL and 1.0 x 10(-9)-6.0 x 10(-6) g/mL for BSA and HSA, respectively. Their detection limits were 1.4 x 10(-8) g/mL and 2.8 x 10(-10) g/mL (S:N = 3), respectively. Synthetic and actual samples were analysed satisfactorily.

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Microdetermination of proteins by Rayleigh light scattering technique with acid green 25

Cited by 63 publications

References 10 publications

Determination of Proteins with Fast Red VR by a Corrected Resonance Light-Scattering Technique

Determination of Proteins with Fast Red VR by a Corrected Resonance Light-Scattering Technique

Voltammetric studies on the interaction of orange G with proteins: analytical applications

Resonance light scattering technique for the determination of proteins with Congo red and Triton X‐100

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