A combined magnetic sector–time‐of‐flight mass spectrometer for structural determination studies by tandem mass spectrometry

Bateman, Robert; Green, M. R.; Grace, S. R.; Clayton, E. G.

doi:10.1002/rcm.1290091302

Cited by 79 publications

(68 citation statements)

References 12 publications

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“…44 The ion source was a standard FAB source with the addition of a nitrogen laser (337 nm), which Ðred through a sapphire window mounted over the ion source housing.…”

Section: Mass Spectrometermentioning

confidence: 99%

High-energy Collision-induced Fragmentation of Complex Oligosaccharides Ionized by Matrix-assisted Laser Desorption/Ionization Mass Spectrometry

Harvey¹,

1997

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The high‐energy CID spectra of the MNa+ ions from 17 underivatized oligosaccharides of the type found attached to asparagine in glycoproteins were examined with a double‐focusing mass spectrometer fitted with a tandem orthogonal time‐of‐flight analyser. Fragment ions were observed throughout the mass range from all compounds and provided considerable structural information in the low‐picomole range. The three types of fragmentation that were observed were glycosidic cleavages, cross‐ring cleavages and the formation of internal cleavage ions. The major glycosidic fragmentations were B‐ and Y‐type cleavages (Domon and Costello nomenclature). B‐cleavages were particularly abundant at GlcNAc residues. Z‐ions were absent when glycosidic linkages occurred at the 6‐position. Cross‐ring cleavages were predominantly of the 1,5X‐type, which provided much sequence and branching information. 3,5A cleavages of the core branching mannose residue were often prominent and provided information on the composition of each of the main antennae. Antenna composition was also reflected by a major internal fragment ion formed by elimination of the two GlcNAc residues of the chitobiose core together with the entire antenna at the 3‐position of the core branching mannose residue. A further loss of GlcNAc as 221 mass units from this ion in the spectra of the hybrid and complex carbohydrates was indicative of the presence of a ‘bisecting’ (4‐linked) GlcNAc substituent. Another prominent internal fragment ion containing a mannose residue and only one GlcNAc, with its substituents, was present in the spectra of the complex sugars when branching of the 3‐antenna occurred. © 1997 by John Wiley & Sons, Ltd.

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“…44 The ion source was a standard FAB source with the addition of a nitrogen laser (337 nm), which Ðred through a sapphire window mounted over the ion source housing.…”

Section: Mass Spectrometermentioning

confidence: 99%

High-energy Collision-induced Fragmentation of Complex Oligosaccharides Ionized by Matrix-assisted Laser Desorption/Ionization Mass Spectrometry

Harvey¹,

1997

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“…Spectra were recorded in the mass range 100-3100 m/z at a scan time of 10 s/decade and at a resolution of 2000 (at 10% valley definition). Daughter ion spectra of selected monoisotopically resolved immonium precursor ions were recorded at 800 eV lab frame collision energy (Bateman et al, 1995) using argon as collision gas. Liquid secondary ion mass spectrometry (LSIMS) of CsI (Merck, Germany) was used to precalibrate the instrument prior to EI-MS analyses.…”

Section: Mass Spectrometrymentioning

confidence: 99%

Glycosphingolipid expression in pig aorta: Identification of possible target antigens for human natural antibodies

Hallberg¹,

Holgersson

Samuelsson³

1998

Glycobiology

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Total non-acid glycosphingolipids were isolated from the aortas of more than 80 pigs. The glycolipids were separated by HPLC, analysed by thin-layer chromatography, and tested for reactivity with monoclonal anti-blood group antibodies. The fractions were structurally characterized by NMR spectroscopy and mass spectrometry. Reactivity with both antiblood group A and H antibodies was seen. The major glycosphingolipid constituents were globotriand globotetraosylceramides and blood group H pentaglycosylceramides based on type 1 and type 2 core saccharide chains. Globopentaosylceramides, blood group H hexaglycosylceramides based on type 4 chain, and blood group A hexaglycosylceramides based on type 1 core chain were also present. Two structures, that may be important targets for human antibodies initiating hyperacute rejection following pig to human xenotransplantation, were present as minor constituents compared to the blood group components. These were Galα1,3neolactotetraosylceramide and a Galα1,3Le x structure. A Le b /Y hexaglycosylceramide was also present.

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“…17. 41 Once again the high duty factor of the TOFMS provides excellent sensitivity and 'simultaneous' detection of fragment ions. The resolution of MS2 is extremely good and relatively unencumbered by kinetic energy released in the fragmentation processes induced between MS1 and MS2.…”

Section: Hybrid Instruments and Ms/tofmsmentioning

confidence: 99%

Perfect Timing: Time-of-flight Mass Spectrometry†

Guilhaus

Mlynski

Selby

1997

Rapid Commun. Mass Spectrom.

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In the 1990s time-of-flight mass spectrometry (TOFMS) has reestablished itself as a mainstream technique in mass spectrometry. There have been several developments which have contributed to this. The development of the technique of matrix-assisted laser desorption/ionization (MALDI), a pulsed ionization method, has provided a user-friendly, low-cost window on the high mass regime for the molecular biologist. The availability of high-speed computers has allowed efficient processing of TOF data on the microsecond time-scale. The emergence of practical ion optical approaches for space, time and velocity focusing have improved the resolving power and sensitivity of TOFMS far beyond its limited performance in previous decades. The technique of time-of-flight mass spectrometry (TOFMS) has returned as a prominent mass analysis method. TOFMS can be advantageous compared to scanning technologies because of its 'unlimited' mass range, high speed and the potential for high duty factors (% of ions formed that are detected). Two important causes for the renewed activity in TOFMS can be identified: (i) The development of and need for new ionization methods capable of generating ions of structural significance from high molecular weight materials. In particular, developments in ion sources for molecular biology provide a strong driving force for TOFMS. Matrix-assisted laser desorption/ionization (MALDI) 1 and electrospray ionization (ESI) 2 have been prominent in this regard. (ii) The facilitating technologies for TOFMS have advanced dramatically during the past decade. These include affordable pulsed lasers, nanosecond digitizers, focal plane detectors and microcomputing power.The convergence of the need for high mass analysis with the availability of the necessary technology has been perfectly timed. But the recent successes of TOFMS must equally be attributed to research directed at overcoming the physical limitations inherent in the TOFMS experiment. Dispersions in the initial position, time and velocity of the ion population severely limited the resolving power of early TOFMS instruments. Inefficient production, gating and detection of ion packets have, until recently, placed considerable constraints on the sensitivity of the TOF mass analyser. The need to form discrete packets of ions has provided a challenge in the coupling of continuous ion sources to TOFMS.The development of the ion mirror (or reflectron) 3 and the orthogonal acceleration time-of-flight mass spectrometer (oa-TOFMS) 4-6 have been key stages in the revival of TOFMS. FACTORS CONTRIBUTING TO TOFMS RENAISSANCEThe simplicity of the physical principles of TOFMS underpin its current successes. The mass-velocity relationship for constant energy ions and the electrostatic force on a charge when combined with Newtonian mechanics provide the foundations of all TOFMS equations:force on a charge in an electric field F = ma Newton's second law a = Eq/m acceleration in a constant electric field where q = charge; V = electrical potential through which an ion having ch...

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A combined magnetic sector–time‐of‐flight mass spectrometer for structural determination studies by tandem mass spectrometry

Cited by 79 publications

References 12 publications

High-energy Collision-induced Fragmentation of Complex Oligosaccharides Ionized by Matrix-assisted Laser Desorption/Ionization Mass Spectrometry

High-energy Collision-induced Fragmentation of Complex Oligosaccharides Ionized by Matrix-assisted Laser Desorption/Ionization Mass Spectrometry

Glycosphingolipid expression in pig aorta: Identification of possible target antigens for human natural antibodies

Perfect Timing: Time-of-flight Mass Spectrometry†

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