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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Published in | Methods in molecular biology (Clifton, N.J.) Vol. 919; p. 215 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
United States
2013
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Subjects | |
Online Access | Get more information |
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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. |
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ISSN: | 1940-6029 |
DOI: | 10.1007/978-1-62703-029-8_20 |