Journal
CARBOHYDRATE RESEARCH
Volume 345, Issue 10, Pages 1486-1491Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.carres.2010.05.012
Keywords
Flow cytometry; Mucin; Lectin; Protein-carbohydrate interaction
Funding
- BBSRC [BBS/E/F/00044452, BBS/E/F/00042268] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BBS/E/F/00042268, BBS/E/F/00044452] Funding Source: researchfish
- Biotechnology and Biological Sciences Research Council [BBS/E/F/00042268, BBS/E/F/00044452] Funding Source: Medline
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The O-glycosylated domains of mucins and mucin-type glycoproteins contain 50-80% of carbohydrate and possess expanded conformations. Herein, we describe a flow cytometry (FCM) method for determining the carbohydrate-binding specificities of lectins to mucin. Biotinylated mucin was immobilized on streptavidin-coated beads, and the binding specificities of the major mucin sugar chains, as determined by GC-MS and MALDI-ToF, were monitored using fluorescein-labeled lectins. The specificities of lectins toward specific biotinylated glycans were determined as controls. The advantage of flexibility, multiparametric data acquisition, speed, sensitivity, and high-throughput capability makes flow cytometry a valuable tool to study diverse interactions between glycans and proteins. (c) 2010 Elsevier Ltd. All rights reserved.
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