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血清淀粉样蛋白A定量质谱免疫分析方法的开发

Development of quantitative mass spectrometric immunoassay for serum amyloid A.

作者信息

Trenchevska Olgica, Yassine Hussein N, Borges Chad R, Nelson Randall W, Nedelkov Dobrin

机构信息

a The Biodesign Institute, Arizona State University , Tempe , AZ , USA.

b Department of Medicine , University of Southern California , Los Angeles , CA , USA.

出版信息

Biomarkers. 2016 Dec;21(8):743-751. doi: 10.1080/1354750X.2016.1201533. Epub 2016 Jul 22.

DOI:10.1080/1354750X.2016.1201533
PMID:27308834
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5253327/
Abstract

OBJECTIVE

Proteins can exist as multiple proteoforms in vivo that can have important roles in physiological and pathological states.

METHODS

We present the development and characterization of mass spectrometric immunoassay (MSIA) for quantitative determination of serum amyloid A (SAA) proteoforms.

RESULTS

Intra- and inter-day precision revealed CVs <10%. Against existing SAA ELISA, the developed MSIA showed good correlation according to the Altman-Bland plot. Individual concentrations of the SAA proteoforms across a cohort of 170 samples revealed 7 diverse SAA polymorphic types and 12 different proteoforms.

CONCLUSION

The new SAA MSIA enables parallel analysis of SAA polymorphisms and quantification of all expressed SAA proteoforms, in a high-throughput and time-efficient manner.

摘要

目的

蛋白质在体内可作为多种蛋白质异构体存在，这些异构体在生理和病理状态中可能发挥重要作用。

方法

我们介绍了用于定量测定血清淀粉样蛋白A（SAA）蛋白质异构体的质谱免疫分析（MSIA）的开发与特性。

结果

日内和日间精密度显示变异系数<10%。根据奥特曼-布兰德图，所开发的MSIA与现有的SAA酶联免疫吸附测定法显示出良好的相关性。对170个样本队列中SAA蛋白质异构体的个体浓度分析揭示了7种不同的SAA多态性类型和12种不同的蛋白质异构体。

结论

新的SAA MSIA能够以高通量和高效省时的方式对SAA多态性进行平行分析，并对所有表达的SAA蛋白质异构体进行定量。

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