<figcaption>A model of erythropoietin, which exists as a mixture of glycosylated variants. This glycoform contains three N-linked oligosaccharides (purple) and one O-linked glycan (pink). Glycans contribute to a large percentage of the overall mass and surface area of glycoproteins. Credit: courtesy of Robert Woods, UGA, Athens</figcaption>
A model of erythropoietin, which exists as a mixture of glycosylated variants. This glycoform contains three N-linked oligosaccharides (purple) and one O-linked glycan (pink). Glycans contribute to a large percentage of the overall mass and surface area of glycoproteins. Credit: courtesy of Robert Woods, UGA, Athens

Researcher:
Karen Abbott, postdoctoral research associate, Complex Carbohydrate Research Center, University of Georgia, Athens

Project:
Breast cancer biomarker discovery

Problem:
Abbott works with proteins whose glycosylation patterns differ in normal versus cancerous cells. She needed a method that could enrich and identify these glycoproteins.

Solution:
Breast cancer epithelial cells express higher levels of an enzyme that creates a specific sugar structure called beta-1,6-branched N-linked oligosaccharide. That modification is absent from normal breast epithelia. Says Abbott, "That means the glycosylation of the protein is the malignant marker, not the...

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