Enzymatic Sequence Analysis of Glycoprotein Glycans

Prime, Sally B.; Shipston, Nigel F.; Merry, Tony

doi:10.1007/978-3-0348-7388-8_12

Cited by 6 publications

(9 citation statements)

References 23 publications

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“…These were prepared essentially by the method described by Prime et al 14 Briefly, the dried glycan was dissolved in dry DMSO (6 ml) to which had been added acetic acid (2 ml). An excess of 2-aminobenzamide was added, followed by sodium cyanoborohydride to give a final concentration of about 1 M. The mixture was heated at 65 °C for 2 h, cooled, applied to a strip (100 3 30 mm) of Whatman 3MM Chr chromatography paper (Whatman International Ltd., Maidstone, Kent, UK) and allowed to dry.…”

Section: Preparation Of Derivativesmentioning

confidence: 99%

Electrospray mass spectrometry and collision-induced fragmentation of 2-aminobenzamide-labelled neutral N-linked glycans

Harvey

2000

Analyst

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The positive ion fragmentation spectra of the singly-and doubly-charged sodiated adducts from high-mannose, hybrid and complex N-linked glycans, labelled at the reducing terminus with 2-aminobenzamide (2-AB), were examined using electrospray ionization and collision-induced decomposition on a hybrid Q-TOF instrument. [M + Na] + ions, whose abundance could be enhanced by operating the ion source at a high cone-voltage, gave the most informative spectra but, because the relative abundance of the singly-charged ions fell as a function of mass to a greater extent than the abundance of the doubly-sodiated ions, the latter were more useful for larger glycans. The spectra were more complicated than those obtained from protonated adducts but simpler than those of the underivatised glycans. Although the spectra from both hydrogen and sodium adducts were dominated by ions formed by B-and Y-type glycosidic cleavages, those from the sodium adducts were more complex and contained additional C and Z ions together with products of cross-ring cleavages yielding linkage information. Many fragment ions were formed via multiple pathways by losses of sugar residues from different regions of the molecule (internal fragments). The presence of the reducing-terminal 2-AB derivative effectively labelled this region of the molecule, thus simplifying spectral interpretation. Structural features identified by this technique included the isobaric monosaccharide composition, presence or absence of a core (reducing-terminal) linked fucose and 'bisecting' (4-linked to the branching core mannose) GlcNAc residue together with information on the branching patterns.

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Section: Preparation Of Derivativesmentioning

confidence: 99%

Electrospray mass spectrometry and collision-induced fragmentation of 2-aminobenzamide-labelled neutral N-linked glycans

Harvey

2000

Analyst

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“…For example, endoS from Streptococcus pyogenes [10] can be used to release biantennary complex-type glycans from glycoproteins such as IgG. [10] Structural identification of the released glycans relies heavily on mass spectrometry and on the use of exoglycosidases to cleave carbohydrate residues from the non-reducing terminus, [11,12] with detection of the products either by fluorescence after suitable labelling, or by mass spectrometry. The exoglycosidase technique provides information on the type and linkage of the removed residues but is less successful in determining branching and fails directly to detect structural features such as the presence of a 'bisecting' GlcNAc residue (β-GlcNAc attached to the 4-position of the core mannose) because of the lack of suitable exoglycosidases.…”

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confidence: 99%

Fragmentation of negative ions from N-linked carbohydrates: Part 6. Glycans containing oneN-acetylglucosamine in the core

Harvey

Edgeworth

Krishna

et al. 2014

Rapid Commun. Mass Spectrom.

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“…The hydrazide conjugation of oligosaccharides was performed based on a procedure previously described by Gouw et al 57 Ten microliters of an oligosaccharide (500 µM in methanol) was mixed with 50 µL of AMCA‐hydrazide solution (1 mM in 70% methanol and 30% acetic acid). The solution was heated to 75 °C for 4 h. The reductive amination of oligosaccharides with AMC was conducted using a procedure reported by Prime et al 58 Briefly, 10 µL of oligosaccharide solution (100 µM in methanol) was mixed with 10 µL of AMC solution (0.5 M in 70% dimethylsulfoxide (DMSO) and 30% acetic acid). The solution was heated to 65 °C for an hour.…”

Section: Methodsmentioning

confidence: 99%

Ultraviolet photodissociation of chromophore‐labeled oligosaccharides via reductive amination and hydrazide conjugation

Brodbelt

2011

J. Mass Spectrom.

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The fragmentation patterns of hydrazide-conjugated and reductively aminated oligosaccharides, including lacto-N-fucopentaoses and lacto-N-difucohexaoses, produced on collisionally induced dissociation (CID) and ultraviolet photodissociation (UVPD) in a quadrupole ion trap are presented. The two derivatization methods generate different cross-ring cleavages on UVPD and CID. UVPD of hydrazide-conjugated oligosaccharides yield predominant (2, 4)A-type cross-ring cleavage ions. In contrast, UVPD of aminated oligosaccharides results mainly in (0, 1)A-type ions. Moreover, more extensive dual-cleavage pathways (i.e. internal fragment ions) were observed on UVPD.

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Enzymatic Sequence Analysis of Glycoprotein Glycans

Cited by 6 publications

References 23 publications

Electrospray mass spectrometry and collision-induced fragmentation of 2-aminobenzamide-labelled neutral N-linked glycans

Electrospray mass spectrometry and collision-induced fragmentation of 2-aminobenzamide-labelled neutral N-linked glycans

Fragmentation of negative ions from N-linked carbohydrates: Part 6. Glycans containing oneN-acetylglucosamine in the core

Ultraviolet photodissociation of chromophore‐labeled oligosaccharides via reductive amination and hydrazide conjugation

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