The high mannose glycans from bovine ribonuclease B isomer characterization by ion trap MS

Prien, Justin M.; Ashline, David J.; Lapadula, Anthony J.; Zhang, Hailong; Reinhold, Vernon N.

doi:10.1016/j.jasms.2008.11.012

Cited by 132 publications

(161 citation statements)

References 16 publications

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“…The starting material from the M5-AEAB fraction was relatively pure with minor contaminants comprised of M6-AEAB (m/z ϭ 1582.8) and possibly one of the isomers of M5-AEAB eluting between 10 and 11 min that was recently described (35). The HPLC profile of the reaction products indicated that the major canonical structure M5-AEAB was unchanged by the GlcNAc-phosphotransferase reaction, which is consistent with M5 being a very poor substrate for the enzyme (36).…”

Section: Purification Of the Phosphodiesters Of Highmentioning

confidence: 80%

See 1 more Smart Citation

Glycan Microarray Analysis of P-type Lectins Reveals Distinct Phosphomannose Glycan Recognition

Song

Lasanajak

Olson

et al. 2009

Journal of Biological Chemistry

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The specificity of the cation-independent and -dependent mannose 6-phosphate receptors (CI-MPR and CD-MPR) for high mannose-type N-glycans of defined structure containing zero, one, or two Man-P-GlcNAc phosphodiester or Man-6-P phosphomonoester residues was determined by analysis on a phosphorylated glycan microarray. Amine-activated glycans were covalently printed on N-hydroxysuccinimide-activated glass slides and interrogated with different concentrations of recombinant CD-MPR or soluble CI-MPR. Neither receptor bound to non-phosphorylated glycans. The CD-MPR bound weakly or undetectably to the phosphodiester derivatives, but strongly to the phosphomonoester-containing glycans with the exception of a single Man7GlcNAc2-R isomer that contained a single Man-6-P residue. By contrast, the CI-MPR bound with high affinity to glycans containing either phospho-mono-or -diesters although, like the CD-MPR, it differentially recognized isomers of phosphorylated Man7GlcNAc2-R. This differential recognition of phosphorylated glycans by the CI-and CD-MPRs has implications for understanding the biosynthesis and targeting of lysosomal hydrolases.

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Section: Purification Of the Phosphodiesters Of Highmentioning

confidence: 80%

“…1E. Phosphorylated derivatives of GAEABs generated from M6, M8, and M9 glycans represent single isomers of their most common or canonical structures, which were described recently (35) and shown in Table 1.…”

Section: Purification Of the Phosphodiesters Of Highmentioning

confidence: 96%

Glycan Microarray Analysis of P-type Lectins Reveals Distinct Phosphomannose Glycan Recognition

Song

Lasanajak

Olson

et al. 2009

Journal of Biological Chemistry

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“…Tandem MS of permethylated glycans carries the advantage that ions formed from cleavage of glycosidic bonds have a unique mass value that distinguishes an internal fragment from a single bond cleavage. Multistage dissociation of permethylated glycans has been used to determine detailed linkage information for saccharide units formed by gas phase disassembly of the glycans (Zhang et al, 2005;Prien et al, 2008Prien et al, , 2009Jiao et al, 2011). The key to multistage dissociation of glycans is the selection of a series of precursor ions that isolate structural branches for subsequent stages.…”

Section: Characterization Of N- O-linked Glycans From Glycoproteinsmentioning

confidence: 99%

Tandem Mass Spectrometry of Tagged and Permethylated Polysaccharides

Yang¹

2012

Tandem Mass Spectrometry - Applications and Principles

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“…Tandem MS (MS/MS or MS N ) analysis can be employed for proteins to further separate a peptide into fragments [58]. For glycans, tandem MS analysis can resolve structural isomers [59] and large number of variations in linkage and branching [60]. Collision induced dissociation (CID) is commonly used to fragment precursor ions for the next round of MS analysis [61].…”

Section: Approach In Glycomicsmentioning

confidence: 99%

Development of Monolithic Column Materials for the Separation and Analysis of Glycans

Alla

Stine

2015

Chromatography

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Monolithic column materials offer great advantages as chromatographic media in bioseparations and as solid-supports in biocatalysis. These single-piece porous materials have an interconnected ligament structure that limits the void volume inside the column, thus increasing the efficiency without sacrificing the permeability. The preparation of monolithic materials is easy, reproducible and has available a wide range of chemistries to utilize. Complex, heterogeneous and isobaric glycan structures require preparation methods that may include glycan release, separation and enrichment prior to a comprehensive and site-specific glycosylation analysis. Monolithic column materials aid that demand, as shown by the results reported by the research works presented in this review. These works include selective capture of glycans and glycoproteins via their interactions with lectins, boronic acids, hydrophobic, and hydrophilic/polar functional groups on monolith surfaces. It also includes immobilization of enzymes trypsin and PNGase F on monoliths to digest and deglycosylate glycoproteins and glycopeptides, respectively. The use of monolithic capillary columns for glycan separations through nano-liquid chromatography (nano-LC) and capillary electrochromatography (CEC) and coupling these columns to MS instruments to create multidimensional systems show the potential in the development of miniaturized, high-throughput and automated systems of glycan separation and analysis.

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The high mannose glycans from bovine ribonuclease B isomer characterization by ion trap MS

Cited by 132 publications

References 16 publications

Glycan Microarray Analysis of P-type Lectins Reveals Distinct Phosphomannose Glycan Recognition

Glycan Microarray Analysis of P-type Lectins Reveals Distinct Phosphomannose Glycan Recognition

Tandem Mass Spectrometry of Tagged and Permethylated Polysaccharides

Development of Monolithic Column Materials for the Separation and Analysis of Glycans

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