Matrix effects on an antigen immobilized format for competitive enzyme immunoassay of salivary testosterone

Mitchell, John S.; Lowe, Tim E.

doi:10.1016/j.jim.2009.07.012

Cited by 24 publications

(16 citation statements)

References 31 publications

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“…Despite enormous advances in immunoassays, the unwanted interference from the matrix (so-called matrix effect) is still an important obstacle to overcome (Selby, 1999). The complex and variable chemical components in food samples might greatly interfere with the immunological reactions, resulting in significantly reduced accuracy and sensitivity, and even false results (Mitchell & Lowe, 2009;Tiwari et al, 2010;Zhang et al, 2007). In past years such matrix interference has been reported in a wide range of food samples, including vegetable, tea, fruit, chocolate, dairy, nuts, confectionery, shellfish, animal muscles and fishes (Liu, Fang, Zhang, Zheng, & Wang, 2009;Naar et al, 2002;Tate & Ward, 2004).…”

Section: Introductionmentioning

confidence: 99%

The matrix interference to the immunoassay of food samples: The effect of some proteins in aquatic products

Wang

Lin

Cao

et al. 2015

Food and Agricultural Immunology

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The elimination of matrix interference is now a task for further development and application of immunoassays. Here the effect of proteins in aquatic samples on immunoassay was investigated by western blotting and competitive indirect enzyme-labeled immunosorbent assay (ci-ELISA). Some proteins in flatfishes interacted with different antibodies, resulting in significant loss of accuracy of the immunoassays. Moreover, these matrix proteins prefer to interact with enzyme-labeled antibodies than label-free ones. Such a matrix protein-immunoglobulin interaction was validated with different fish and shrimp samples and similar results were observed, which demonstrated a universal significance of the protein-induced matrix interference to immunoassays. Besides, the strategies to prevent such interference were preliminarily discussed.

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Section: Introductionmentioning

confidence: 99%

The matrix interference to the immunoassay of food samples: The effect of some proteins in aquatic products

Wang

Lin

Cao

et al. 2015

Food and Agricultural Immunology

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“…After the development of new rat monoclonal antibodies with different synthesized haptens, a coating antigen ELISA format was developed for the detection of AHLs [18]. An indirect competitive ELISA with the use of a coating antigen is frequently applied and appropriate for the detection of small molecules [19]. In comparison to the SPR sensor, the ELISA microtiter plate was coated with the conjugate HSL2-BSA-r2, and after a washing step, the preincubated analyte-antibody mixtures were added in serial concentrations to the coated plate.…”

Section: Analytesmentioning

confidence: 99%

Comparative surface plasmon resonance and enzyme-linked immunosorbent assay characterisation of a monoclonal antibody with N-acyl homoserine lactones

Wöllner

Chen

Kremmer

et al. 2010

Analytica Chimica Acta

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“…Therefore, several studies were conducted on the immobilization of antigens. However these studies were only concerned with enzyme linked immunosorbent assay [9].…”

Section: Introductionmentioning

confidence: 99%

A Novel Method of Immobilizing Antigens on Gold Electrode for Immunosensing

Uyen¹,

Gajovic‐Eichelmann²,

Bier³

et al. 2015

Comm. in Phys.

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Abstract. An antigen modified gold electrode based on a self-assembled lipoic acid monolayer has been developed. The contact angle measurement and cyclic voltammetry confirm the formation of a dense self-assembled monolayer on gold from 100 mM lipoic acid in ethanol. The electrochemical behavior shows a stable activity in a range of potential from -0.2 V to 0.65 V vs. Ag/AgCl. By applying a potential of 1 V vs. Ag/AgCl the monolayer is completely removed by oxidative desorption and a clean gold surface re-established. This allows for an easy renewal of the gold surface and recycling of modified immunosensor chips. This lipoic acid monolayer was covalently functionalized with a small molecule antigen synthesized from progesterone-3-(O-carboxymethyl)oxime and 4,7,10-trioxa-1,13 tridecanediamine to form a well ordered, low unspecific binding, antigen layer for an antibody-antigen interaction study.The effectiveness of antigen -antibody binding reaction was demonstrated by fluorescence imaging using a fluorescence-labeled antiprogesterone antibody as the binding partner.

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Matrix effects on an antigen immobilized format for competitive enzyme immunoassay of salivary testosterone

Cited by 24 publications

References 31 publications

The matrix interference to the immunoassay of food samples: The effect of some proteins in aquatic products

The matrix interference to the immunoassay of food samples: The effect of some proteins in aquatic products

Comparative surface plasmon resonance and enzyme-linked immunosorbent assay characterisation of a monoclonal antibody with N-acyl homoserine lactones

A Novel Method of Immobilizing Antigens on Gold Electrode for Immunosensing

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