Exploring the binding profiles of ConA, boronic acid and WGA by MALDI-TOF/TOF MS and magnetic particles☆

Sparbier, Katrin; Wenzel, Thomas J.; Kostrzewa, Markus

doi:10.1016/j.jchromb.2006.06.028

Cited by 82 publications

(69 citation statements)

References 13 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…These difficulties are evidenced by the range of techniques developed for removing contaminants including, for example, the use of various types of resin and other adsorbing materials [1][2][3][4], porous graphitized carbon [5][6][7], various membranes [8,9], lectins [10,11], immobilized boronic acids [10,12], and drop dialysis [13]. In our laboratory, Nafion 117 [8] and other membranes are routinely used but, even though these sometimes give spectacular improvements in signals [14], on other occasions they make little or no difference to the detection of glycans.…”

Section: Introductionmentioning

confidence: 99%

Ion Mobility Mass Spectrometry for Extracting Spectra of N-Glycans Directly from Incubation Mixtures Following Glycan Release: Application to Glycans from Engineered Glycoforms of Intact, Folded HIV gp120

Harvey

Sobott

Crispin

et al. 2011

J. Am. Soc. Mass Spectrom.

View full text Add to dashboard Cite

The analysis of glycosylation from native biological sources is often frustrated by the low abundances of available material. Here, ion mobility combined with electrospray ionization mass spectrometry have been used to extract the spectra of N-glycans released with PNGase F from a serial titration of recombinantly expressed envelope glycoprotein, gp120, from the human immunodeficiency virus (HIV). Analysis was also performed on gp120 expressed in the α-mannosidase inhibitor, and in a matched mammalian cell line deficient in GlcNAc transferase I. Without ion mobility separation, ESI spectra frequently contained no observable ions from the glycans whereas ions from other compounds such as detergents and residual buffer salts were abundant. After ion mobility separation on a Waters T-wave ion mobility mass spectrometer, the N-glycans fell into a unique region of the ion mobility/m/z plot allowing their profiles to be extracted with good signal:noise ratios. This method allowed N-glycan profiles to be extracted from crude incubation mixtures with no clean-up even in the presence of surfactants such as NP40. Furthermore, this technique allowed clear profiles to be obtained from sub-microgram amounts of glycoprotein. Glycan profiles were similar to those generated by MALDI-TOF MS although they were more susceptible to double charging and fragmentation. Structural analysis could be accomplished by MS/MS experiments in either positive or negative ion mode but negative ion mode gave the most informative spectra and provided a reliable approach to the analysis of glycans from small amounts of glycoprotein.

show abstract

Section: Introductionmentioning

confidence: 99%

Ion Mobility Mass Spectrometry for Extracting Spectra of N-Glycans Directly from Incubation Mixtures Following Glycan Release: Application to Glycans from Engineered Glycoforms of Intact, Folded HIV gp120

Harvey

Sobott

Crispin

et al. 2011

J. Am. Soc. Mass Spectrom.

View full text Add to dashboard Cite

show abstract

“…Une autre approche a été présentée par M. Kostrzewa pour capturer les glycoprotéines contenues dans le plasma. Cette méthode consiste à utiliser des microparticules magnétiques sur lesquelles sont greffées des lectines ou des acides boroniques [6]. Les protéines ainsi piégées sont ensuite digérées par la trypsine, puis analysées par LC-MALDI-MS/MS.…”

Section: Avancées En Glycoprotéomiquesunclassified

Quand la protéomique s’attaque aux modifications post-traductionnelles…

Delcourt

2007

Med Sci (Paris)

View full text Add to dashboard Cite

“…To the other side, even if the technology for profiling the proteins and even simple post-translational modifications were approaching maturity [22,23], the most abundant post translational modification, glycosylation, still remains practically unexplored [24,25]. This is misleading and resulting from the fact that glycomics researchers profile glycan structures but ignore the proteins from which they came, and proteomics researchers profile proteins while ignoring the appended glycans [26][27][28][29].…”

Section: Introductionmentioning

confidence: 99%

Can Microfluidics boost the Map of Glycome Code?

Simone¹

2014

J Glycomics Lipidomics

View full text Add to dashboard Cite

Exploring the binding profiles of ConA, boronic acid and WGA by MALDI-TOF/TOF MS and magnetic particles☆

Cited by 82 publications

References 13 publications

Ion Mobility Mass Spectrometry for Extracting Spectra of N-Glycans Directly from Incubation Mixtures Following Glycan Release: Application to Glycans from Engineered Glycoforms of Intact, Folded HIV gp120

Ion Mobility Mass Spectrometry for Extracting Spectra of N-Glycans Directly from Incubation Mixtures Following Glycan Release: Application to Glycans from Engineered Glycoforms of Intact, Folded HIV gp120

Quand la protéomique s’attaque aux modifications post-traductionnelles…

Can Microfluidics boost the Map of Glycome Code?

Contact Info

Product

Resources

About