LOGIN TO YOUR ACCOUNT

Username
Password
Remember Me
Or use your Academic/Social account:

CREATE AN ACCOUNT

Or use your Academic/Social account:

Congratulations!

You have just completed your registration at OpenAire.

Before you can login to the site, you will need to activate your account. An e-mail will be sent to you with the proper instructions.

Important!

Please note that this site is currently undergoing Beta testing.
Any new content you create is not guaranteed to be present to the final version of the site upon release.

Thank you for your patience,
OpenAire Dev Team.

Close This Message

CREATE AN ACCOUNT

Name:
Username:
Password:
Verify Password:
E-mail:
Verify E-mail:
*All Fields Are Required.
Please Verify You Are Human:
fbtwitterlinkedinvimeoflicker grey 14rssslideshare1
Harvey, David J.; Scarff, Charlotte A.; Edgeworth, Matthew; Pagel, Kevin; Thalassinos, Konstantinos; Struwe, Weston B.; Crispin, Max; Scrivens, Jim (2016)
Languages: English
Types: Article
Subjects: CID, N-linked carbohydrates, T-wave ion mobility, complex N-glycans, hybrid N-glycans, isomers, negative ion, Article
Nitrogen collisional cross sections (CCSs) of hybrid and complex glycans released from the glycoproteins IgG, gp120 (from human immunodeficiency virus), ovalbumin, α1-acid glycoprotein and thyroglobulin were measured with a travelling-wave ion mobility mass spectrometer using dextran as the calibrant. The utility of this instrument for isomer separation was also investigated. Some isomers, such as Man3 GlcNAc3 from chicken ovalbumin and Man3 GlcNAc3 Fuc1 from thyroglobulin could be partially resolved and identified by their negative ion fragmentation spectra obtained by collision-induced decomposition (CID). Several other larger glycans, however, although existing as isomers, produced only asymmetric rather than separated arrival time distributions (ATDs). Nevertheless, in these cases, isomers could often be detected by plotting extracted fragment ATDs of diagnostic fragment ions from the negative ion CID spectra obtained in the transfer cell of the Waters Synapt mass spectrometer. Coincidence in the drift times of all fragment ions with an asymmetric ATD profile in this work, and in the related earlier paper on high-mannose glycans, usually suggested that separations were because of conformers or anomers, whereas symmetrical ATDs of fragments showing differences in drift times indicated isomer separation. Although some significant differences in CCSs were found for the smaller isomeric glycans, the differences found for the larger compounds were usually too small to be analytically useful. Possible correlations between CCSs and structural types were also investigated, and it was found that complex glycans tended to have slightly smaller CCSs than high-mannose glycans of comparable molecular weight. In addition, biantennary glycans containing a core fucose and/or a bisecting GlcNAc residue fell on different mobility-m/z trend lines to those glycans not so substituted with both of these substituents contributing to larger CCSs. Copyright © 2016 John Wiley & Sons, Ltd.
  • The results below are discovered through our pilot algorithms. Let us know how we are doing!

    • 1) Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK. 2) Department of Biological Sciences, University of Warwick, Coventry, CV47AL, UK.
    • 3) Current address, Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, University of Leeds, Leeds, LS2 9JT, UK.
    • 4) Current address, MedImmune, Sir Aaron Klug Building, Granta Park, Cambridge, CB21 6GH, UK 5) Institute of Chemistry and Biochemistry, Freie Universität Berlin, Takustrasse. 3, 14159 Berlin, Germany.
    • 6) Institute of Structural and Molecular Biology, Department of Biological Sciences, Birkbeck College, University of London, London, WC1E 7HX, UK.
    • Communications: Dr David J. Harvey, Oxford Glycobiology Institute, Department of Biochemistry, South Parks Road, Oxford, OX1 3QU, UK.
    • Tel. (44) (0) 1865 275750 Fax. (44) (0) 1865 275216 e-mail
    • [23] Harvey DJ, Scrivens JH, Holland R, Williams JP, Wormald MR. Ion-mobility separation coupled with negative ion fragmentation of N-linked carbohydrates. Paper presented at the 56th ASMS Conference on Mass Spectrometry, Denver, 2008: Proceedings CD MOG 09.10.
    • [24] Hermannová M, Iordache Adistributions of product ions reveal isomeric ratio of deprotonated molecules in ion mobility mass spectrometry of hyaluronan-derived oligosaccharides. J. Mass Spectrom. 2015; 50: 854 863.
    • [25] Harvey DJ, Abrahams JL. Fragmentation and ion mobility properties of negative ions from Nlinked carbohydrates: Part 7: Reduced glycans. Rapid Commun. Mass Spectrom. 2016; 30: 627-634.
    • [26] Harvey DJ, Sobott F, Crispin M, Wrobel A, Bonomelli C, Vasiljevic S, Scanlan CN, Scarff C, Thalassinos K, Scrivens JH. Ion mobility mass spectrometry for extracting spectra of Nglycans directly from incubation mixtures following glycan release: Application to glycans from engineered glycoforms of intact, folded HIV gp120. J. Am. Soc. Mass Spectrom. 2011; 22: 568-581.
    • [27] Harvey DJ, Crispin M, Bonomelli C, Scrivens JH. Ion mobility mass spectrometry for ion recovery and clean-up of MS and MS/MS spectra obtained from low abundance viral samples. J. Am. Soc. Mass Spectrom. 2015; 26: 1754-1767.
    • [28] Fenn LS, McLean JA. Biomolecular structural separations by ion mobility mass spectrometry. Anal. Bioanal. Chem. 2008; 391: 905-909.
    • [29] Fenn LS, McLean JA. Enhanced carbohydrate structural selectivity in ion mobility-mass spectrometry analyses by boronic acid derivatization. Chem. Commun. 2008: 5505-5507.
    • [30] Fenn LS, Kliman M, Mahsut A, Zhao SR, McLean JA. Characterizing ion mobility-mass spectrometry conformation space for the analysis of complex biological samples. Anal. Bioanal. Chem. 2009; 394: 235-244.
    • [31] Li H, Bendiak B, Siems WF, Gang DR, Hill Jr. HH. Ion mobility-mass correlation trend line separation of glycoprotein digests without deglycosylation. Int. J. Ion Mobil. Spectrom. 2013; 16: 105-115.
    • [32] Harvey DJ, Scarff CA, Edgeworth M, Crispin M, Scanlan CN, Sobott F, Allman S, Baruah K, Pritchard L, Scrivens JH. Travelling wave ion mobility and negative ion fragmentation for the structural determination of N-linked glycans. Electrophoresis 2013; 34: 2368-2378.
    • [33] Patel T, Bruce J, Merry A, Bigge C, Wormald M, Jaques A, Parekh R. Use of hydrazine to release in intact and unreduced form both N- and O-linked oligosaccharides from glycoproteins. Biochemistry 1993; 32: 679-693.
    • [34] Wing DR, Field MC, Schmitz B, Thor G, Dwek RA, Schachner MS, Rademacher TW. The use of large-scale hydrazinolysis in the preparation of N-linked oligosaccharide libraries: application to brain tissue. Glycoconj. J. 1992; 9: 293-301.
    • [35] de Waard P, Koorevaar A, Kamerling JP, Vliegenthart JFG. Structure determination by 1H NMR spectroscopy of (sulfated) sialylated N-linked carbohydrate chains released from porcine thyroglobulin by peptide-N4-(N-acetyl- -glucosaminyl)asparagine amidase-F. J. Biol. Chem. 1991; 266: 4237-4243.
    • [36] Kamerling JP, Rijkse I, Maas AAM, van Kuik JA, Vliegenthart JFG. Sulfated N-linked carbohydrate chains in porcine thyroglobulin. FEBS Letts. 1988; 241: 246-250.
    • [37] Da Silva MLC, Stubbs HJ, Tamura T, Rice KG. 1H-NMR characterization of a hen ovalbumin tyrosinamide N-linked oligosaccharide library. Arch. Biochem. Biophys. 1995; 318: 465-475.
    • [38] Harvey DJ, Wing DR, Küster B, Wilson IBH. Composition of N-linked carbohydrates from ovalbumin and co-purified glycoproteins. J. Am. Soc. Mass Spectrom. 2000; 11: 564-571.
    • [39] Yang Y, Barendregt A, Kamerling JP, Heck AJR. Analyzing protein micro-heterogeneity in chicken ovalbumin by high-resolution native mass spectrometry exposes qualitatively and semi-quantitatively 59 proteoforms. Anal. Chem. 2013; 85: 12037-12045.
    • [40] Green ED, Adelt G, Baenziger JU, Wilson S, van Halbeek H. The asparagine-linked oligosaccharides on bovine fetuin. Structural analysis of N-glycanase-released oligosaccharides by 500- Megahertz 1H-NMR spectroscopy. J. Biol. Chem. 1988; 263: 18253-18268.
    • [41] Fournet B, Montreuil J, Strecker G, Dorland L, Haverkamp J, Vliegenthart JFG, Binette JP, Schmid K. Determination of the primary structures of 16 asialo-carbohydrate units derived from human plasma 1-acid glycoprotein by 360 MHz 1H NMR spectroscopy and permethylation analysis. Biochemistry 1978; 17: 5206-5214.
    • [42] Küster B, Hunter AP, Wheeler SF, Dwek RA, Harvey DJ. Structural determination of N-linked carbohydrates by matrix-assisted laser desorption/ionization mass spectrometry following enzymatic release within sodium dodecyl sulfate-polyacrylamide electrophoresis gels: application to species-specific glycosylation of 1-acid glycoprotein. Electrophoresis 1998; 19: 1950-1959.
    • [43] Küster B, Wheeler SF, Hunter AP, Dwek RA, Harvey DJ. Sequencing of N-linked oligosaccharides directly from protein gels: In-gel deglycosylation followed by matrix-assisted laser desorption/ionization mass spectrometry and normal-phase high performance liquid chromatography. Anal. Biochem. 1997; 250: 82-101.
    • [44] Börnsen KO, Mohr MD, Widmer HM. Ion exchange and purification of carbohydrates on a Nafion(R) membrane as a new sample pretreatment for matrix-assisted laser desorptionionization mass spectrometry. Rapid Commun. Mass Spectrom. 1995; 9: 1031-1034.
    • [45] Giles K, Pringle SD, Worthington KR, Little D, Wildgoose JL, Bateman RH. Applications of a travelling wave-based radio-frequency-only stacked ring ion guide. Rapid Commun. Mass Spectrom. 2004; 18: 2401-2414.
    • [46] Hernández H, Robinson CV. Determining the stoichiometry and interactions of macromolecular assemblies from mass spectrometry. Nat. Protocols 2007; 2: 715 - 726.
    • [47] Domon B, Costello CE. A systematic nomenclature for carbohydrate fragmentations in FABMS/MS spectra of glycoconjugates. Glycoconj. J. 1988; 5: 397-409.
    • [48] Harvey DJ. Electrospray mass spectrometry and collision-induced fragmentation of 2- aminobenzamide-labelled neutral N-linked glycans. The Analyst 2000; 125: 609-617.
    • [49] Pringle SD, Giles K, Wildgoose JL, Williams JP, Slade SE, Thalassinos K, Bateman RH, Bowers MT, Scrivens JH. An investigation of the mobility separation of some peptide and protein ions using a new hybrid quadrupole/travelling wave IMS/oa-ToF instrument. Int. J. Mass Spectrom. 2007; 261: 1-12.
    • [50] Bush MF, Hall Z, Giles K, Hoyes J, Robinson CV, Ruotolo BT. Collision cross sections of proteins and their complexes: A calibration framework and database for gas-phase structural biology. Anal. Chem. 2010; 82: 9557-9565.
    • [51] Pagel K, Natan E, Hall Z, Fersht AR, Robinson CV. Intrinsically disordered p53 and its complexes populate compact conformations in the gas phase. Angew. Chem. Int. Ed. 2013; 52: 361-365.
    • [52] Pagel K, Harvey DJ. Ion mobility mass spectrometry of complex carbohydrates - collision cross sections of sodiated N-linked glycans. Anal. Chem. 2013; 85: 5138-5145.
    • [53] Hofmann J, Struwe WB, Scarff CA, Scrivens JH, Harvey DJ, Pagel K. Estimating collision cross sections of negatively charged N-glycans using travelling wave ion mobility-mass spectrometry. Anal. Chem. 2014; 86: 10789-10795.
    • [54] Thalassinos K, Grabenauer M, Slade SE, Hilton GR, Bowers MT, Scrivens JH. Characterization of phosphorylated peptides using traveling wave-based and drift cell ion mobility mass spectrometry. Anal. Chem. 2009; 81: 248-254.
    • [55] May JC, Goodwin CR, Lareau NM, Leaptrot KL, Morris CB, Kurulugama RT, Mordehai A, Klein C, Barry W, Darland E, Overney G, Imatani K, Stafford GC, Fjeldsted JC, McLean JA. Conformational ordering of biomolecules in the gas phase: Nitrogen collision cross sections measured on a prototype high resolution drift tube ion mobility-mass spectrometer. Anal. Chem. 2014; 86: 2107-2116.
    • [56] Campbell MP, Struwe W, Pagel K, Benesch JLP, Harvey DJ. GlycoMob - an ion mobility mass spectrometry database. Glycobiology 2015; 25: 1275-1276.
    • [57] Li H, Bendiak B, Siems WF, Gang DR, Hill J, Herbert H. Ion mobility mass spectrometry analysis of isomeric disaccharide precursor, product and cluster ions. Rapid Commun. Mass Spectrom. 2013; 27: 2699 2709.
    • [58] Gaye MM, Kurulugama R, Clemmer DE. Investigating carbohydrate isomers by IMS-CID-IMSMS: Precursor and fragment ion cross-sections. Analyst 2015; 140: 6922-6932.
    • [59] Harvey DJ, Scarff CA, Crispin M, Scanlan CN, Bonomelli C, Scrivens JH. MALDI-MS/MS with traveling wave ion mobility for the structural analysis of N-linked glycans. J. Am. Soc. Mass Spectrom. 2012; 23: 1955-1966.
    • [60] Saba J, Zumwalt A, Meitei NS, Apte A, Viner R. Automated glycan structural isomer differentiation using a bioinformatics tool. Proceedings of the 59th ASMS Conference on Mass Spectrometry and Allied Topics, Denver 2011: TP08 170.
    • [61] Harvey DJ, Edgeworth M, Krishna BA, Bonomelli C, Allman S, Crispin M, Scrivens JH. Fragmentation of negative ions from N-linked carbohydrates: Part 6: Glycans containing one N-acetylglucosamine in the core. Rapid Commun. Mass Spectrom. 2014; 28: 2008 2018.
    • [62] Harvey DJ, Crispin M, Scanlan C, Singer BB, Lucka L, Chang VT, Radcliffe CM, Thobhani S, Yuen C-T, Rudd PM. Differentiation between isomeric triantennary N-linked glycans by negative ion tandem mass spectrometry and confirmation of glycans containing galactose
  • Inferred research data

    The results below are discovered through our pilot algorithms. Let us know how we are doing!

    Title Trust
    69
    69%
  • No similar publications.

Share - Bookmark

Funded by projects

  • NIH | Center for HIV/AIDS Vaccine...

Cite this article