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Titel
nES GEMMA analysis of lectins and their interactions with glycoproteins separation, detection, and sampling of noncovalent biospecific complexes / Nicole Y. Engel, Victor U. Weiss, Martina Marchetti-Deschmann, Günter Allmaier
VerfasserEngel, Nicole Yvonne ; Weiss, Victor ; Marchetti-Deschmann, Martina ; Allmaier, Günter
Erschienen in
Journal of The American Society for Mass Spectrometry, New York, 2017,
Erschienen2017
Ausgabe
Published version
Umfang1 Online-Ressource (10 Seiten, 7 Seiten) : Diagramme
SpracheEnglisch
DokumenttypAufsatz in einer Zeitschrift
Schlagwörter (EN)Lectin / Glycoproteinn / ES GEMMA / CE-on-a-chip / Electrophoresis
Projekt-/ReportnummerTRP 29-N20
ISSN1879-1123
URNurn:nbn:at:at-ubtuw:3-2604 Persistent Identifier (URN)
DOI10.1007/s13361-016-1483-0 
Zugriffsbeschränkung
 Das Werk ist frei verfügbar
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nES GEMMA analysis of lectins and their interactions with glycoproteins separation, detection, and sampling of noncovalent biospecific complexes [1.87 mb]
Supplementary material (pdf) [1.08 mb]
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Zusammenfassung (Englisch)

In order to better understand biological events, lectinglycoprotein interactions are of interest. The possibility to gather more information than the mere positive or negative response for interactions brought mass spectrometry into the center of many research fields. The presented work shows the potential of a nano-electrospray gas-phase electrophoretic mobility molecular analyzer (nES GEMMA) to detect weak, noncovalent, biospecific interactions besides still unbound glycoproteins and unreacted lectins without prior liquid phase separation. First results for Sambucus nigra agglutinin, concanavalin A, and wheat germ agglutinin and their retained noncovalent interactions with glycoproteins in the gas phase are presented. Electrophoretic mobility diameters (EMDs) were obtained by nES GEMMA for all interaction partners correlating very well with molecular masses determined by matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) of the individual molecules. Moreover, EMDs measured for the lectinglycoprotein complexes were in good accordance with theoretically calculated mass values. Special focus was laid on complex formation for different lectin concentrations and binding specificities to evaluate the method with respect to results obtained in the liquid phase. The latter was addressed by capillary electrophoresis on-a-chip (CE-on-a-chip). Of exceptional interest was the fact that the formed complexes could be sampled according to their size onto nitrocellulose membranes after gas-phase separation. Subsequent immunological investigation further proved that the collected complex actually retained its native structure throughout nES GEMMA analysis and sampling.

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CC-BY-Lizenz (4.0)Creative Commons Namensnennung 4.0 International Lizenz