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  • Title: Matrix-assisted laser desorption/ionization tandem mass spectrometry of N-glycans derivatized with isonicotinic hydrazide and its biotinylated form.
    Author: Bank S, Heller E, Memmel E, Seibel J, Holzgrabe U, Kapková P.
    Journal: Rapid Commun Mass Spectrom; 2014 Aug 15; 28(15):1745-56. PubMed ID: 24975255.
    Abstract:
    RATIONALE: Successful structural characterization of glycans often requires derivatization prior to mass spectrometric analysis. Here we report on a new derivatization reagent for glycans, biotinylated isonicotinic hydrazide, allowing glycan analysis by both mass spectrometry (MS) and biochemically. Fragmentation behavior in MS and its use in structural elucidation were investigated and compared with other labels. METHODS: Glycans, released from ribonuclease B and ovalbumin, were derivatized with hydrazine labels (isoniazid (INH), biotinylated isonicotinic hydrazide (BINH) and biotinamidocaproylhydrazide (BACH)). In addition, native counterparts and 2-aminobenzamide (2-AB) derivatives were prepared. Comparative matrix-assisted laser desorption/ionization tandem time-of-flight (MALDI TOF/TOF) experiments were carried out to investigate the fragmentation pattern of the derivatives. Finally, the capability of BINH derivatives to bind lectins was explored. RESULTS: Generally, derivatization provided beneficial enhancement in the mass spectrometric signal intensity as compared to native counterparts. The mass spectrometric fragmentation varied with the kind of label used. The most significant structure-revealing ions (cross-ring cleavages) were observed in the spectra of BINH derivatives, whereas mainly glycosidic cleavages were found with native form of glycans and 2-AB derivatives. CONCLUSIONS: Hydrazine derivatization provided the means to obtain structurally informative fragment ions. Due to BINH derivatization, specific fragments of the isomers allowed the identification of diverse glycans. The derivatization reaction can be carried out without the need for purification. The biotin residue of BINH enabled for biochemical studies, i.e. protein-glycan interactions.
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