Linked Life Data

20217867

Source:http://linkedlifedata.com/resource/pubmed/id/20217867

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2010-7-12
pubmed:abstractText
Protein glycosylation is one of the most important PTMs in biological organism. Lectins such as concanavalin A (Con A) have been widely applied to N-glycosylated protein investigation. In this study, we developed Con A-immobilized magnetic nanoparticles for selective separation of glycoproteins. At first, a facile immobilization of Con A on aminophenylboronic acid-functionalized magnetic nanoparticles was performed by forming boronic acid-sugar-Con A bond in sandwich structure using methyl alpha-D-mannopyranoside as an intermedium. The selective capture ability of Con A-modified magnetic nanoparticles for glycoproteins was tested using standard glycoproteins and cell lysate of human hepatocelluar carcinoma cell line 7703. In total 184 glycosylated sites were detected within 172 different glycopeptides corresponding to 101 glycoproteins. Also, the regeneration of the protein-immobilized nanoparticles can easily be performed taking advantage of the reversible binding mechanism between boronic acid and sugar chain. The experiment results demonstrated that Con A-modified magnetic nanoparticles by the facile and low-cost synthesis provided a convenient and efficient enrichment approach for glycoproteins, and are promising candidates for large-scale glycoproteomic research in complicated biological samples.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1615-9861
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2000-14
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Concanavalin A-immobilized magnetic nanoparticles for selective enrichment of glycoproteins and application to glycoproteomics in hepatocelluar carcinoma cell line.
pubmed:affiliation
Department of Chemistry and Institute of Biomedical Sciences, Fudan University, Shanghai, PR China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't