Profiling the morphological distribution of O-linked oligosaccharides

Zhang, Jinhua; Xie, Yongming; Hedrick, Jerry L.; Lebrilla, Carlito B.

doi:10.1016/j.ab.2004.07.012

Cited by 27 publications

(26 citation statements)

References 25 publications

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“…Over the last decade, Lebrilla et al developed an LC-MS method for the analysis of HMO samples, based on a nanoHPLC Chip/TOF MS approach [7,8,14,15,22,[50][51][52] using graphitized carbon chromatography (GCC). GCC is stable, has a long life [53] and is effective for the separation of both neutral and acidic oligosaccharides, including isomers [54]. In Figure 10a, a base peak chromatogram of an HMO sample is shown [50].…”

Section: Lc Maldi Ms and Lc-ms Of Human Milk Oligosaccharidesmentioning

confidence: 99%

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Challenges in Separations of Proteins and Small Biomolecules and the Role of Modern Mass Spectroscopy Tools for Solving Them, as Well as Bypassing Them, in Structural Analytical Studies of Complex Biomolecular Mixtures

Haramija

2018

Separations

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State-of-the-art purification of biomolecules, as well as separation of complex omic mixtures, is crucial for modern biomedical research. Mass spectroscopy (MS) represents a technique that both requires very clean biomedical samples and can substantially assist liquid chromatography (LC) separations, using either LC-MS or LC-MS/MS methods available. Here, a brief overview of the applicability of LC-MS/MS methodology for structural analyses of complex omic mixtures without prior purification of each sample component will be given. When necessary bioinformatic tools are available, these can be carried out quite quickly. However, manual data analysis of such complex mixtures is typically very slow. On the other hand, the need for high-level purity of protein samples for modern biomedical research will be discussed. Often, modification of protein purification protocols is needed, or additional purification steps may be either required or preferred. In the context of mass spectroscopy-related biomedical research, purification of pmol and subpmol amounts of biomedical samples, as well as commercial availability of pmol amounts of purified standards will be discussed.

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Section: Lc Maldi Ms and Lc-ms Of Human Milk Oligosaccharidesmentioning

confidence: 99%

“…GCC is stable, has a long life [53] and is effective for the separation of both neutral and acidic oligosaccharides, including isomers [54]. In Figure 10a, a base peak chromatogram of an HMO sample is shown [50].…”

Section: Lc Maldi Ms and Lc-ms Of Human Milk Oligosaccharidesmentioning

confidence: 99%

Challenges in Separations of Proteins and Small Biomolecules and the Role of Modern Mass Spectroscopy Tools for Solving Them, as Well as Bypassing Them, in Structural Analytical Studies of Complex Biomolecular Mixtures

Haramija

2018

Separations

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“…Supernatant containing N-glycans was purified using Sep-Pak C18 equilibrated sequentially with acetonitrile and ultrapure water. N-glycans eluted from the Sep-Pak and supernatant containing O-glycan alditols from reductive ␤-elimination were further purified using Carbograph cartridges as described in Zhang et al, 33 except neutral and acidic oligosaccharides were eluted in 1 batch using 40% (vol/vol) acetonitrile containing 0.1% trifluoroacetic acid. Eluates were dried in vacuum.…”

Section: Glycan Removal and Purificationmentioning

confidence: 99%

Glycoforms of human endothelial CD34 that bind L-selectin carry sulfated sialyl Lewis x capped O- and N-glycans

Mir

Helin

Skarp

et al. 2009

Blood

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Endothelial sialomucin CD34 functions as an L-selectin ligand mediating lymphocyte extravasation only when properly glycosylated to express a sulfated carbohydrate epitope, 6-sulfo sialyl Lewis x (6-sulfo SLe x ). It is thought that multivalent 6-sulfo SLe x expression promotes highaffinity binding to L-selectin by enhancing avidity. However, the reported low amount of 6-sulfo SLe x in total human CD34 is inconsistent with this model and prompted us to re-evaluate CD34 glycosyl-

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“…Moreover, these columns are unaffected by strongly acidic or alkaline conditions and can be used throughout the entire pH range with a wide range of solvents. Thus far, these columns have been utilized in conjunction with MS for the analysis of glycans derived from different samples, including egg jelly surrounding Xenopus laevis eggs [53,75,76], human bronchial epithelial cell cultures [77], membrane proteins from premature aging HuchinsonGilford progeria syndrome fibroblasts [78], human tear fluid [79], and human plasma [80]. Moreover, microliter flow rates were employed in all these applications, allowing only the detection of structures present in abundance.…”

Section: 2mentioning

confidence: 99%

New hyphenated methodologies in high‐sensitivity glycoprotein analysis

Novotný

Mechref

2005

J of Separation Science

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High-sensitivity glycoprotein analyses are of particular interest in modern biomedical and clinical research, as well as in the development of recombinant protein products. The evolution of new hyphenated methodologies in high-sensitivity glycoprotein analysis is highlighted in this thematic review. These methodologies include, in particular, capillary LC/MALDI/TOF/TOF MS in conjunction with online permethylation platform, and silica-based lectin microcolumns interfaced to MS. The potential of these methodologies in glycomic and glycoproteomic analysis is demonstrated for model glycoproteins as well as total glycomes and glycoproteomes derived from biological samples. Additionally, the applications of CE-MS, CEC, and nanoLC with graphitized carbon in the areas of glycomics and glycoproteomics are described.

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Profiling the morphological distribution of O-linked oligosaccharides

Cited by 27 publications

References 25 publications

Challenges in Separations of Proteins and Small Biomolecules and the Role of Modern Mass Spectroscopy Tools for Solving Them, as Well as Bypassing Them, in Structural Analytical Studies of Complex Biomolecular Mixtures

Challenges in Separations of Proteins and Small Biomolecules and the Role of Modern Mass Spectroscopy Tools for Solving Them, as Well as Bypassing Them, in Structural Analytical Studies of Complex Biomolecular Mixtures

Glycoforms of human endothelial CD34 that bind L-selectin carry sulfated sialyl Lewis x capped O- and N-glycans

New hyphenated methodologies in high‐sensitivity glycoprotein analysis

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