Immunoaffinity, capillary electrophoresis, and statistics for studying intact alpha 1-acid glycoprotein isoforms as an atherothrombosis biomarker

Variations in the amino acid sequence, glycosylation, and/or other posttranslational modifications in glycoproteins give rise to different molecules of the glycoprotein called forms. Qualitative and/or quantitative alterations in these forms are related to pathophysiological situations in the indivi...

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Bibliographic Details
Published inMethods in molecular biology (Clifton, N.J.) Vol. 919; p. 215
Main Authors Puerta, Angel, Martin-Alvarez, Pedro J, Ongay, Sara, Diez-Masa, Jose C, de Frutos, Mercedes
Format Journal Article
LanguageEnglish
Published United States 2013
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Summary:Variations in the amino acid sequence, glycosylation, and/or other posttranslational modifications in glycoproteins give rise to different molecules of the glycoprotein called forms. Qualitative and/or quantitative alterations in these forms are related to pathophysiological situations in the individuals. In this study, a methodology to analyze these differences in forms of the alpha 1-acid glycoprotein (AGP) between healthy individuals and patients with two different vascular diseases is detailed. The whole methodology includes a sample preparation method based on immunochromatography, a capillary electrophoresis method for separation of AGP peaks (isoforms), and statistical methods (Linear Discriminant Analysis) for sample classification. As a result, it is shown that the methodology proposed allows studying the role of AGP isoforms as potential vascular disease biomarkers.
ISSN:1940-6029
DOI:10.1007/978-1-62703-029-8_20