A sensitive enzyme immunoassay for measuring cotinine in passive smokers

Park, Sunyoung; Lee, Dong Hoon; Park, Jae Gahb; Lee, Yong Tae; Chung, Junho

doi:10.1016/j.cca.2010.04.027

Cited by 49 publications

(58 citation statements)

References 25 publications

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“…A high-affinity anti-cotinine antibody was originally generated by our group to develop a super-sensitive enzyme immunoassay for the detection of second-hand smoking exposure (27). The antibody has k on , k off , and K D values of 2.6 × 10 6 M -1 ㆍs -1 , 1.3 × 10 -5 s -1 and 4.9 × 10 -12 M, respectively (28).…”

Section: Cotinine As An Ideal Hapten To Link the Antibody And Chemicamentioning

confidence: 99%

In vitro and in vivo application of anti-cotinine antibody and cotinine-conjugated compounds

2014

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The combination of a high-affinity antibody to a hapten, and hapten-conjugated compounds, can provide an alternative to the direct chemical cross-linking of the antibody and compounds. An optimal hapten for in vitro use is one that is absent in biological systems. For in vivo applications, additional characteristics such as pharmacological safety and physiological inertness would be beneficial. Additionally, methods for cross-linking the hapten to various chemical compounds should be available. Cotinine, a major metabolite of nicotine, is considered advantageous in these aspects. A high-affinity anti-cotinine recombinant antibody has recently become available, and can be converted into various formats, including a bispecific antibody. The bispecific anti-cotinine antibody was successfully applied to immunoblot, enzyme immunoassay, immunoaffinity purification, and pre-targeted in vivo radioimmunoimaging. The anti-cotinine IgG molecule could be complexed with aptamers to form a novel affinity unit, and extended the in vivo half-life of aptamers, opening up the possibility of applying the same strategy to therapeutic peptides and chemical compounds. [BMB Reports 2014; 47(3): 130-134]

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Section: Cotinine As An Ideal Hapten To Link the Antibody And Chemicamentioning

confidence: 99%

In vitro and in vivo application of anti-cotinine antibody and cotinine-conjugated compounds

2014

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“…To estimate this parameter, the working standard was serially diluted in assay buffer, and each dilution was analyzed in 5 replicates in the same analytical run. 12 Additionally, the ability of the TR-FIA to distinguish between healthy and diseased animals was tested in serum, saliva, and meat juice samples by clinical validation. For this purpose, SAA was determined in each specimen type from the control (n = 20) and diseased (n = 20) pigs detailed above, and results were compared.…”

Section: Immunoassay Validationmentioning

confidence: 99%

Fast measurement of serum amyloid A in different specimens from swine by using a new one-step time-resolved fluorescent immunoassay

et al. 2011

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Abstract. The objective of the present study was to develop a one-step, fast, competitive time-resolved fluorescent immunoassay to determine porcine serum amyloid A (SAA) by using species-specific reagents. The assay consisted of an all-in-one format involving only 55 min of incubation that was adapted and validated for use in 3 different specimens: serum, saliva, and meat juice. The method had overall within-and between-run coefficients of variation under 8% and 12%, respectively, and coefficients of determination higher than 0.93 for linearity under dilution analysis for all specimens. The limits of detection were 0.32 mg/l, 0.28 mg/l, and 1.74 mg/l for serum, saliva, and meat juice measurements, respectively. Upper and lower limits of quantification were determined for each sample type and resulted in wide assay ranges that allowed a precise SAA measurement in all the fluids investigated. Statistically significant differences (P = 0.0004 for serum and P < 0.0001 for the saliva and meat juice samples) in SAA levels were found when healthy (n = 20) and diseased (n = 20) pigs were compared. The obtained results indicate that this fast, sensitive, and robust assay for SAA measurement could be of use to determine health and welfare status in swine by employing alternative samples to serum.Key words: Meat juice; pigs; saliva; serum amyloid A; time-resolved fluorescent immunoassay. performance and sensitivity were significantly improved with respect to the commercial assay. 16 However, this method, as is common with most ELISAs, determination of results can be time-consuming and the methodology cumbersome for routine analysis.

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“…Several methods have been reported for the determination of NIC, COT and related alkaloids in various biological fluids, and those include immunoassays [18][19][20][21], gas chromatography (GC) coupled to either flame ionisation (FID) [22] or mass spectrometric (MS) detection [1,12,[23][24][25][26], high-performance liquid chromatography (LC) coupled to UV detector [27,28] or MS [7,16,[29][30][31][32][33][34][35][36]. Hydrophilic interaction chromatography-tandem mass spectrometry (HILIC-MS/MS) methods have been also reported [33].…”

Section: Introductionmentioning

confidence: 99%

Determination of biomarkers of tobacco smoke exposure in oral fluid using solid-phase extraction and gas chromatography–tandem mass spectrometry

Fonseca

Moreno

Magalhães

et al. 2012

Journal of Chromatography B

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A sensitive enzyme immunoassay for measuring cotinine in passive smokers

Cited by 49 publications

References 25 publications

In vitro and in vivo application of anti-cotinine antibody and cotinine-conjugated compounds

In vitro and in vivo application of anti-cotinine antibody and cotinine-conjugated compounds

Fast measurement of serum amyloid A in different specimens from swine by using a new one-step time-resolved fluorescent immunoassay

Determination of biomarkers of tobacco smoke exposure in oral fluid using solid-phase extraction and gas chromatography–tandem mass spectrometry

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