N-Glycan profile analysis of transferrin using a microfluidic compact disc and MALDI-MS
Number of Authors: 4
2016 (English)In: Analusis, ISSN 1618-2642, E-ISSN 1618-2650, Vol. 408, no 17, 4765-4776 p.Article in journal (Refereed) Published
It has been known for a long time that diseases can be associated with changes to the glycosylation of specific proteins. This has been shown for cancer, immunological disorders, and neurodegenerative diseases. The possibility of using the glycosylation patterns of proteins as biomarkers for disease would be a great asset for clinical research or diagnosis. There is at present a lack of rapid, automated, and cost-efficient analytical techniques for the determination of the glycosylation of specific serum proteins. We have developed a method for determining the glycosylation pattern of proteins based on the affinity capture of a specific serum protein, the enzymatic release of the N-linked glycans, and the analysis of the glycan pattern using MALDI-MS. All sample preparation is performed in a disposable centrifugal microfluidic disc. The sample preparation is miniaturized, requiring only 1 mu L of sample per determination, and automated with the possibility of processing 54 samples in parallel in 3.5 h. We have developed a method for the glycosylation pattern analysis of transferrin. The method has been tested on serum samples from chronic alcohol abusers and a control group. Also, a SIMCA model was created and evaluated to discriminate between the two groups.
Place, publisher, year, edition, pages
2016. Vol. 408, no 17, 4765-4776 p.
Glycan pattern, Glycomics, N-linked oligosaccharide, Transferrin, Microfluidic, MALDI-MS
Analytical Chemistry Biochemistry and Molecular Biology
IdentifiersURN: urn:nbn:se:su:diva-132558DOI: 10.1007/s00216-016-9570-4ISI: 000378725200025PubMedID: 27137515OAI: oai:DiVA.org:su-132558DiVA: diva2:953613