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Ionisation and fragmentation of complex glycans with a quadrupole time-of-flight mass spectrometer fitted with a matrix-assisted laser desorption/ionisation ion source.
Rapid Commun Mass Spectrom. 2000; 14(22):2135-42.RC

Abstract

This paper reports the use of an experimental matrix-assisted laser desorption/ionisation (MALDI) ion source fitted to a quadrupole time-of-flight (Q-Tof) mass spectrometer for the analysis of carbohydrates, particularly the N-linked glycans from glycoproteins. Earlier work on the Q-Tof instrument, using electrospray ionisation, gave excellent MS/MS spectra, particularly from the [M + Na]+ ions, but suffered from the major disadvantages that the signal was often split between singly and multiply charged ions and that sensitivity fell dramatically as the molecular weight of the carbohydrate rose. The MALDI ion source did not suffer from these problems and the instrument produced excellent MS and MS/MS spectra from small amounts of complex, underivatised glycans as well as those derivatised at the reducing terminus. Positive ion MS spectra of sialylated glycans recorded on the new instrument were much less complex than those recorded with a conventional MALDI-TOF instrument because of the absence of ions resulting from metastable (post-source decay, (PSD)) fragmentations occurring in the flight tube. However, considerable fragmentation by loss of sialic acid still occurred. MS/MS spectra of the [M + Na]+ ions from all compounds were almost identical to those recorded earlier with the electrospray-Q-Tof combination and far superior to MALDI-PSD spectra recorded with reflectron-TOF instruments. Spectra are shown for neutral and sialylated N-linked glycans from chicken ovalbumin, riboflavin binding protein, alpha1-acid glycoprotein, bovine fetuin and ribonuclease B, both as free glycans and as those derivatised at their reducing termini. The technique was applied to the structural determination of N-linked glycans from human secretory IgA and Apo-B 100 from human low-density lipoprotein.

Authors+Show Affiliations

Glycobiology Institute, Department of Biochemistry, University of Oxford, UK. dh@glycob.ox.ac.ukNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

11114021

Citation

Harvey, D J., et al. "Ionisation and Fragmentation of Complex Glycans With a Quadrupole Time-of-flight Mass Spectrometer Fitted With a Matrix-assisted Laser Desorption/ionisation Ion Source." Rapid Communications in Mass Spectrometry : RCM, vol. 14, no. 22, 2000, pp. 2135-42.
Harvey DJ, Bateman RH, Bordoli RS, et al. Ionisation and fragmentation of complex glycans with a quadrupole time-of-flight mass spectrometer fitted with a matrix-assisted laser desorption/ionisation ion source. Rapid Commun Mass Spectrom. 2000;14(22):2135-42.
Harvey, D. J., Bateman, R. H., Bordoli, R. S., & Tyldesley, R. (2000). Ionisation and fragmentation of complex glycans with a quadrupole time-of-flight mass spectrometer fitted with a matrix-assisted laser desorption/ionisation ion source. Rapid Communications in Mass Spectrometry : RCM, 14(22), 2135-42.
Harvey DJ, et al. Ionisation and Fragmentation of Complex Glycans With a Quadrupole Time-of-flight Mass Spectrometer Fitted With a Matrix-assisted Laser Desorption/ionisation Ion Source. Rapid Commun Mass Spectrom. 2000;14(22):2135-42. PubMed PMID: 11114021.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Ionisation and fragmentation of complex glycans with a quadrupole time-of-flight mass spectrometer fitted with a matrix-assisted laser desorption/ionisation ion source. AU - Harvey,D J, AU - Bateman,R H, AU - Bordoli,R S, AU - Tyldesley,R, PY - 2000/12/13/pubmed PY - 2001/3/7/medline PY - 2000/12/13/entrez SP - 2135 EP - 42 JF - Rapid communications in mass spectrometry : RCM JO - Rapid Commun Mass Spectrom VL - 14 IS - 22 N2 - This paper reports the use of an experimental matrix-assisted laser desorption/ionisation (MALDI) ion source fitted to a quadrupole time-of-flight (Q-Tof) mass spectrometer for the analysis of carbohydrates, particularly the N-linked glycans from glycoproteins. Earlier work on the Q-Tof instrument, using electrospray ionisation, gave excellent MS/MS spectra, particularly from the [M + Na]+ ions, but suffered from the major disadvantages that the signal was often split between singly and multiply charged ions and that sensitivity fell dramatically as the molecular weight of the carbohydrate rose. The MALDI ion source did not suffer from these problems and the instrument produced excellent MS and MS/MS spectra from small amounts of complex, underivatised glycans as well as those derivatised at the reducing terminus. Positive ion MS spectra of sialylated glycans recorded on the new instrument were much less complex than those recorded with a conventional MALDI-TOF instrument because of the absence of ions resulting from metastable (post-source decay, (PSD)) fragmentations occurring in the flight tube. However, considerable fragmentation by loss of sialic acid still occurred. MS/MS spectra of the [M + Na]+ ions from all compounds were almost identical to those recorded earlier with the electrospray-Q-Tof combination and far superior to MALDI-PSD spectra recorded with reflectron-TOF instruments. Spectra are shown for neutral and sialylated N-linked glycans from chicken ovalbumin, riboflavin binding protein, alpha1-acid glycoprotein, bovine fetuin and ribonuclease B, both as free glycans and as those derivatised at their reducing termini. The technique was applied to the structural determination of N-linked glycans from human secretory IgA and Apo-B 100 from human low-density lipoprotein. SN - 0951-4198 UR - https://www.unboundmedicine.com/medline/citation/11114021/Ionisation_and_fragmentation_of_complex_glycans_with_a_quadrupole_time_of_flight_mass_spectrometer_fitted_with_a_matrix_assisted_laser_desorption/ionisation_ion_source_ L2 - https://doi.org/10.1002/1097-0231(20001130)14:22<2135::AID-RCM143>3.0.CO;2-# DB - PRIME DP - Unbound Medicine ER -