nano electrospray ion source  (Thermo Fisher)


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    Structured Review

    Thermo Fisher nano electrospray ion source
    Mass spectra of Fe−8HQ (L) coordination complexes detected in solutions by <t>nano-ESI−MS</t> <t>(nano-electrospray−mass</t> spectrometry); positive ionization mode. The solutions were prepared by mixing of 8-hydroxyquinoline (8HQ) solution with ( a ) Fe II or ( b ) Fe III solutions in molar ratio of metal to ligand of 1:2.
    Nano Electrospray Ion Source, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 167 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Price from $9.99 to $1999.99
    nano electrospray ion source - by Bioz Stars, 2020-07
    90/100 stars

    Images

    1) Product Images from "Antioxidant Properties and the Formation of Iron Coordination Complexes of 8-Hydroxyquinoline"

    Article Title: Antioxidant Properties and the Formation of Iron Coordination Complexes of 8-Hydroxyquinoline

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms19123917

    Mass spectra of Fe−8HQ (L) coordination complexes detected in solutions by nano-ESI−MS (nano-electrospray−mass spectrometry); positive ionization mode. The solutions were prepared by mixing of 8-hydroxyquinoline (8HQ) solution with ( a ) Fe II or ( b ) Fe III solutions in molar ratio of metal to ligand of 1:2.
    Figure Legend Snippet: Mass spectra of Fe−8HQ (L) coordination complexes detected in solutions by nano-ESI−MS (nano-electrospray−mass spectrometry); positive ionization mode. The solutions were prepared by mixing of 8-hydroxyquinoline (8HQ) solution with ( a ) Fe II or ( b ) Fe III solutions in molar ratio of metal to ligand of 1:2.

    Techniques Used: Mass Spectrometry

    Related Articles

    High Performance Liquid Chromatography:

    Article Title: Capture of micrococcin biosynthetic intermediates reveals C-terminal processing as an obligatory step for in vivo maturation
    Article Snippet: .. A Thermo Scientific EASY-Spray source and column (PepMap, C18, 3 µm, 100A, 75 µm × 15 µm) was used with a Waters Nano Acquity HPLC system and a Thermo Scientific LTQ-Orbitrap XL mass spectrometer for LCMS analysis. .. Zip-Tipped samples were diluted as appropriate in 0.1% formic acid in water and injected onto the column, which was maintained at 45 °C.

    Flow Cytometry:

    Article Title: Developing a Multiplexed Quantitative Cross-linking Mass Spectrometry Platform for Comparative Structural Analysis of Protein Complexes
    Article Snippet: .. Mixed peptide samples were analyzed utilizing a Thermo Scientific™ EASY-nLC™ 1000 UPLC system coupled on-line to a Thermo Scientific™ Orbitrap Fusion Lumos™ MS. A Thermo Scientific™ EASY-Spray™ source with a 25 cm × 75 μm PepMap EASY-Spray Column was used to separate peptides over a 55 min acetonitrile gradient of 6% to 35% at a flow rate of 300 nL/min. .. Each mixed peptide sample was analyzed using three individual acquisition methods: 1) a targeted ID-MS3 acquisition optimized for DSSO cross-linked peptide identification, 2) a MultiNotch MS3 acquisition featuring synchronous precursor selection (SPS) , and 3) a combined ID-MS3 targeted acquisition with additional SPS-MS3 for all precursor ions selected for ID-MS3 .

    Liquid Chromatography with Mass Spectroscopy:

    Article Title: Capture of micrococcin biosynthetic intermediates reveals C-terminal processing as an obligatory step for in vivo maturation
    Article Snippet: .. A Thermo Scientific EASY-Spray source and column (PepMap, C18, 3 µm, 100A, 75 µm × 15 µm) was used with a Waters Nano Acquity HPLC system and a Thermo Scientific LTQ-Orbitrap XL mass spectrometer for LCMS analysis. .. Zip-Tipped samples were diluted as appropriate in 0.1% formic acid in water and injected onto the column, which was maintained at 45 °C.

    Generated:

    Article Title: Identification of Arenin, a Novel Kunitz-Like Polypeptide from the Skin Secretions of Dryophytes arenicolor
    Article Snippet: .. Eluents A (0.1% FA) and B (90% ACN, 0.1% FA) were used to establish the following 60-min gradient: 7–18% B for 30 min, 18–32% B for 15 min, 32–50% B for 4 min, 50–90% B for 1 min, 90–5% B for 0.1 min, 5% B for 7.9 min, 5–7% B for 2 min. Spray was generated using a Thermo Scientific EASY-Spray source (Bremen, Germany) at 1.75 kV. .. QExactive mass spectrometer was set to positive mode for data acquisition with Xcalibur 3.0.63 software (Thermo Fisher Scientific Inc., Bremen, Germany) software alternating between full Fourier transform-mass spectrometry (FT-MS) (350−1600 m / z , resolution 75,000, with 1 μscan per spectrum) and FT-MS/MS (resolution 35000, with 1 μscan per spectrum).

    Quantitation Assay:

    Article Title: Protein lysine de-2-hydroxyisobutyrylation by CobB in prokaryotes
    Article Snippet: .. PRM analysis Quantitation using PRM was performed on an Orbitrap Q Exactive Plus mass spectrometer with an EASY-Spray source coupled to a Nano-LC system (EASY-nLC 1000, Thermo Fisher Scientific, Waltham, MA). ..

    Mass Spectrometry:

    Article Title: Protein lysine de-2-hydroxyisobutyrylation by CobB in prokaryotes
    Article Snippet: .. PRM analysis Quantitation using PRM was performed on an Orbitrap Q Exactive Plus mass spectrometer with an EASY-Spray source coupled to a Nano-LC system (EASY-nLC 1000, Thermo Fisher Scientific, Waltham, MA). ..

    Article Title: The RstAB System Impacts Virulence, Motility, Cell Morphology, Penicillin Tolerance and Production of Type II Secretion System-Dependent Factors in the Fish and Human Pathogen Photobacterium damselae subsp. damselae
    Article Snippet: .. The ressolubilized peptides were analyzed by liquid chromatography (LC) coupled to an Orbitrap Q-Exactive mass spectrometer (Thermo Scientific) using a nano spray ionization source (Easy-Spray, Thermo Scientific). .. Reverse phase peptide separation was performed with an Ultimate 3000 system (Thermo Scientific) fitted with a trapping cartridge (Acclaim PepMap C18 100Å, 5 mm × 300 μm i.d., 160454, Thermo Scientific) in a mobile phase of 2% ACN, 0.1% FA at 10 μL min-1 .

    Article Title: Developing a Multiplexed Quantitative Cross-linking Mass Spectrometry Platform for Comparative Structural Analysis of Protein Complexes
    Article Snippet: .. Mixed peptide samples were analyzed utilizing a Thermo Scientific™ EASY-nLC™ 1000 UPLC system coupled on-line to a Thermo Scientific™ Orbitrap Fusion Lumos™ MS. A Thermo Scientific™ EASY-Spray™ source with a 25 cm × 75 μm PepMap EASY-Spray Column was used to separate peptides over a 55 min acetonitrile gradient of 6% to 35% at a flow rate of 300 nL/min. .. Each mixed peptide sample was analyzed using three individual acquisition methods: 1) a targeted ID-MS3 acquisition optimized for DSSO cross-linked peptide identification, 2) a MultiNotch MS3 acquisition featuring synchronous precursor selection (SPS) , and 3) a combined ID-MS3 targeted acquisition with additional SPS-MS3 for all precursor ions selected for ID-MS3 .

    Article Title: Capture of micrococcin biosynthetic intermediates reveals C-terminal processing as an obligatory step for in vivo maturation
    Article Snippet: .. A Thermo Scientific EASY-Spray source and column (PepMap, C18, 3 µm, 100A, 75 µm × 15 µm) was used with a Waters Nano Acquity HPLC system and a Thermo Scientific LTQ-Orbitrap XL mass spectrometer for LCMS analysis. .. Zip-Tipped samples were diluted as appropriate in 0.1% formic acid in water and injected onto the column, which was maintained at 45 °C.

    Article Title: A Proteomic Approach to Identify Alterations in the Small Ubiquitin-like Modifier (SUMO) Network during Controlled Mechanical Ventilation in Rat Diaphragm Muscle *
    Article Snippet: .. The peptides from each gel section were analyzed using a Q Exactive HF Orbitrap mass spectrometer (Thermo Fisher Scientific, Bremen, Germany) equipped with an EASY-Spray ion source (Thermo Fisher Scientific). .. The peptides were separated by reversed phase LC using a Dionex UltiMate 3000 RSLC nanosystem (Thermo Fisher Scientific).

    Article Title: Cytoplasmic glycoengineering of Apx toxin fragments in the development of Actinobacillus pleuropneumoniae glycoconjugate vaccines
    Article Snippet: .. The eluted peptides from C18 column LC eluant were sprayed into the mass spectrometer by means of an Easy-Spray source (Thermo Fisher Scientific Inc.). ..

    Liquid Chromatography:

    Article Title: The RstAB System Impacts Virulence, Motility, Cell Morphology, Penicillin Tolerance and Production of Type II Secretion System-Dependent Factors in the Fish and Human Pathogen Photobacterium damselae subsp. damselae
    Article Snippet: .. The ressolubilized peptides were analyzed by liquid chromatography (LC) coupled to an Orbitrap Q-Exactive mass spectrometer (Thermo Scientific) using a nano spray ionization source (Easy-Spray, Thermo Scientific). .. Reverse phase peptide separation was performed with an Ultimate 3000 system (Thermo Scientific) fitted with a trapping cartridge (Acclaim PepMap C18 100Å, 5 mm × 300 μm i.d., 160454, Thermo Scientific) in a mobile phase of 2% ACN, 0.1% FA at 10 μL min-1 .

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    Thermo Fisher nano spray esi ion source
    Reproducibility test for the integrated <t>Micro-CF/nano-HPLC-ESI-MS/MS.</t> Equal amounts of the sample were analyzed. The tandem mass spectrum obtained at 19.43 min in (A) is shown in (C). The tandem mass spectrum obtained at 19.33 min in (B) is shown in (D).
    Nano Spray Esi Ion Source, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher ltq orbitrap xl
    Properties of LC-MS and MS/MS data recorded from the reference sample. Dilution series of the in-gel digested reference sample analyzed on three hybrid MS instruments <t>(LTQ-FT,</t> LTQ-FT Ultra, and <t>LTQ-Orbitrap</t> XL); data points in A–C are either the means ± S.D. of three (0.1–100 fmol) or two (300 fmol) experiments or represent a single measurement (1000 fmol), respectively. A , number of fragment ion spectra recorded along a 30-min aqueous-organic nano-HPLC gradient as a function of loaded reference protein. Note the pronounced saturation of MS/MS spectra recording with both LTQ-FT configurations starting at 100 fmol. B , number of MS/MS spectra (recorded on LTQ-Orbitrap XL) assigned to indicated protein components of the reference sample. Note the marked variation among individual proteins, as well as pronounced discontinuity and saturation. C , TICs recorded in the experiments in A . The dashed line represents result of a linear regression ( m = 1.25) fitted to the slope of the TICs at loads ≥10 fmol; asymptotes of TICs at loads below ∼3 fmol reflect nonpeptide background signals. D , XICs determined for individual laminin A precursor ions on the LTQ-Orbitrap XL plotted over the load (S.D. omitted for clarity). Signal intensities span more than 6 orders of magnitude with an apparent detection threshold of ∼1000 intensity units ( dashed green line ). The top 20% of precursor ions selected by linear correlation ranking of their XICs (see text and “Experimental Procedures”) are colored in pink . Of the remaining precursor ion profiles, the 10 most intense ones are depicted in black .
    Ltq Orbitrap Xl, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 567 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Thermo Fisher nano electrospray ion source
    Mass spectra of Fe−8HQ (L) coordination complexes detected in solutions by <t>nano-ESI−MS</t> <t>(nano-electrospray−mass</t> spectrometry); positive ionization mode. The solutions were prepared by mixing of 8-hydroxyquinoline (8HQ) solution with ( a ) Fe II or ( b ) Fe III solutions in molar ratio of metal to ligand of 1:2.
    Nano Electrospray Ion Source, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 167 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nano electrospray ion source/product/Thermo Fisher
    Average 93 stars, based on 167 article reviews
    Price from $9.99 to $1999.99
    nano electrospray ion source - by Bioz Stars, 2020-07
    93/100 stars
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    88
    Thermo Fisher nano esi ion source
    Positive ion mode <t>nano-ESI-MS/MS</t> sequencing of permethyl rhFVIIa N -glycans. ( A ) MS/MS product ion profile of the doubly charged doubly sodiated precursor ion at m / z 1227.0913, corresponding to a monosialylated biantennary (6 ppm mass accuracy) N-glycan; ( B ) MS/MS product ion profile of the doubly charged doubly sodiated precursor ion at m / z 1401.1893, corresponding to a monosialylated bifucosylated biantennary N -glycan (1 ppm mass accuracy); ( C ) MS/MS product ion profile of the doubly charged triply sodiated precursor ion at m / z 1076.9753 corresponding to the most intense oligomannose structure, i.e. Man 6 -P-GlcNAc (2 ppm mass accuracy). The glycan representation was made according to the nomenclature of the “Consortium of Functional Glycomics” (CFG).
    Nano Esi Ion Source, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 88/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Reproducibility test for the integrated Micro-CF/nano-HPLC-ESI-MS/MS. Equal amounts of the sample were analyzed. The tandem mass spectrum obtained at 19.43 min in (A) is shown in (C). The tandem mass spectrum obtained at 19.33 min in (B) is shown in (D).

    Journal: Journal of chromatography. A

    Article Title: Micro - Proteome Analysis Using Micro-Chromatofocusing In Intact Protein Separations

    doi: 10.1016/j.chroma.2008.03.065

    Figure Lengend Snippet: Reproducibility test for the integrated Micro-CF/nano-HPLC-ESI-MS/MS. Equal amounts of the sample were analyzed. The tandem mass spectrum obtained at 19.43 min in (A) is shown in (C). The tandem mass spectrum obtained at 19.33 min in (B) is shown in (D).

    Article Snippet: The digested peptide mixture was analyzed by nano-flow reverse-phase LC/MS/MS using the LTQ mass spectrometer with a nano-spray ESI ion source (Thermo, San Jose, CA).

    Techniques: High Performance Liquid Chromatography, Mass Spectrometry

    Properties of LC-MS and MS/MS data recorded from the reference sample. Dilution series of the in-gel digested reference sample analyzed on three hybrid MS instruments (LTQ-FT, LTQ-FT Ultra, and LTQ-Orbitrap XL); data points in A–C are either the means ± S.D. of three (0.1–100 fmol) or two (300 fmol) experiments or represent a single measurement (1000 fmol), respectively. A , number of fragment ion spectra recorded along a 30-min aqueous-organic nano-HPLC gradient as a function of loaded reference protein. Note the pronounced saturation of MS/MS spectra recording with both LTQ-FT configurations starting at 100 fmol. B , number of MS/MS spectra (recorded on LTQ-Orbitrap XL) assigned to indicated protein components of the reference sample. Note the marked variation among individual proteins, as well as pronounced discontinuity and saturation. C , TICs recorded in the experiments in A . The dashed line represents result of a linear regression ( m = 1.25) fitted to the slope of the TICs at loads ≥10 fmol; asymptotes of TICs at loads below ∼3 fmol reflect nonpeptide background signals. D , XICs determined for individual laminin A precursor ions on the LTQ-Orbitrap XL plotted over the load (S.D. omitted for clarity). Signal intensities span more than 6 orders of magnitude with an apparent detection threshold of ∼1000 intensity units ( dashed green line ). The top 20% of precursor ions selected by linear correlation ranking of their XICs (see text and “Experimental Procedures”) are colored in pink . Of the remaining precursor ion profiles, the 10 most intense ones are depicted in black .

    Journal: Molecular & Cellular Proteomics : MCP

    Article Title: Extending the Dynamic Range of Label-free Mass Spectrometric Quantification of Affinity Purifications *

    doi: 10.1074/mcp.M111.007955

    Figure Lengend Snippet: Properties of LC-MS and MS/MS data recorded from the reference sample. Dilution series of the in-gel digested reference sample analyzed on three hybrid MS instruments (LTQ-FT, LTQ-FT Ultra, and LTQ-Orbitrap XL); data points in A–C are either the means ± S.D. of three (0.1–100 fmol) or two (300 fmol) experiments or represent a single measurement (1000 fmol), respectively. A , number of fragment ion spectra recorded along a 30-min aqueous-organic nano-HPLC gradient as a function of loaded reference protein. Note the pronounced saturation of MS/MS spectra recording with both LTQ-FT configurations starting at 100 fmol. B , number of MS/MS spectra (recorded on LTQ-Orbitrap XL) assigned to indicated protein components of the reference sample. Note the marked variation among individual proteins, as well as pronounced discontinuity and saturation. C , TICs recorded in the experiments in A . The dashed line represents result of a linear regression ( m = 1.25) fitted to the slope of the TICs at loads ≥10 fmol; asymptotes of TICs at loads below ∼3 fmol reflect nonpeptide background signals. D , XICs determined for individual laminin A precursor ions on the LTQ-Orbitrap XL plotted over the load (S.D. omitted for clarity). Signal intensities span more than 6 orders of magnitude with an apparent detection threshold of ∼1000 intensity units ( dashed green line ). The top 20% of precursor ions selected by linear correlation ranking of their XICs (see text and “Experimental Procedures”) are colored in pink . Of the remaining precursor ion profiles, the 10 most intense ones are depicted in black .

    Article Snippet: Nano-LC-MS/MS analysis of in-gel digested samples was performed on three different high resolution hybrid ion trap instruments: the LTQ-FT, the upgraded LTQ-FT Ultra, and the LTQ-Orbitrap XL (all Thermo Scientific with Proxeon nano-electrospray ion source).

    Techniques: Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry, High Performance Liquid Chromatography

    Validation of the TopCorr-PV method. Dilutions of the reference sample (amounts of 0.1, 1, 10, 100, and 1000 fmol for each protein) were spiked into a constant protein background and analyzed on an LTQ-Orbitrap XL (1/10 of each sample, three independent sample series). A , relative amounts of the indicated reference proteins determined with the TopCorr-PV method (medians of one to six top-ranked peptide PVs individually normalized to their total sum; means ± SDs of three (six for 100 fmol) replicate samples). The dashed lines indicate expected protein amounts, and the asterisks refer to values based on just one experiment or PV value. B , abundance norm ) of the reference proteins shown in A (means ± S.D. as in A ); respective values of consistently identified and quantified proteins of the background are shown as gray lines (protein profiles, S.D. values omitted for clarity; profile for trypsin is shown in black ). Background proteins cover an abundance range of ∼10 4 corresponding to ∼0.1–100 fmol of the reference proteins. The high values obtained for albumin at 0.1 fmol result from background contamination in the samples. C , histogram plots of rPVs as obtained from the M1–M4 mixtures of solubilized E. coli ). The histogram bars reflect rPVs obtained from the medians of the three to six top-ranked peptide PVs averaged from three replicate samples. Left panel , summary of all E. coli protein rPVs (total of 311 values) from M1:M2, M1:M3, and M1:M4; three right panels , rat, mouse, or human protein rPVs from the indicated mixture ratios. The lines are the results of a Gaussian function fitted to the data; fit parameters peak and half-width (nonlogarithmic values) were 1.02 and 1.29 ( E. coli 1:1; left panel ), 0.083 and 1.53, 0.0056 and 2.00, and 0.0012 and 3.25 for rat brain 1:10, 1:100, and 1:1000, respectively.

    Journal: Molecular & Cellular Proteomics : MCP

    Article Title: Extending the Dynamic Range of Label-free Mass Spectrometric Quantification of Affinity Purifications *

    doi: 10.1074/mcp.M111.007955

    Figure Lengend Snippet: Validation of the TopCorr-PV method. Dilutions of the reference sample (amounts of 0.1, 1, 10, 100, and 1000 fmol for each protein) were spiked into a constant protein background and analyzed on an LTQ-Orbitrap XL (1/10 of each sample, three independent sample series). A , relative amounts of the indicated reference proteins determined with the TopCorr-PV method (medians of one to six top-ranked peptide PVs individually normalized to their total sum; means ± SDs of three (six for 100 fmol) replicate samples). The dashed lines indicate expected protein amounts, and the asterisks refer to values based on just one experiment or PV value. B , abundance norm ) of the reference proteins shown in A (means ± S.D. as in A ); respective values of consistently identified and quantified proteins of the background are shown as gray lines (protein profiles, S.D. values omitted for clarity; profile for trypsin is shown in black ). Background proteins cover an abundance range of ∼10 4 corresponding to ∼0.1–100 fmol of the reference proteins. The high values obtained for albumin at 0.1 fmol result from background contamination in the samples. C , histogram plots of rPVs as obtained from the M1–M4 mixtures of solubilized E. coli ). The histogram bars reflect rPVs obtained from the medians of the three to six top-ranked peptide PVs averaged from three replicate samples. Left panel , summary of all E. coli protein rPVs (total of 311 values) from M1:M2, M1:M3, and M1:M4; three right panels , rat, mouse, or human protein rPVs from the indicated mixture ratios. The lines are the results of a Gaussian function fitted to the data; fit parameters peak and half-width (nonlogarithmic values) were 1.02 and 1.29 ( E. coli 1:1; left panel ), 0.083 and 1.53, 0.0056 and 2.00, and 0.0012 and 3.25 for rat brain 1:10, 1:100, and 1:1000, respectively.

    Article Snippet: Nano-LC-MS/MS analysis of in-gel digested samples was performed on three different high resolution hybrid ion trap instruments: the LTQ-FT, the upgraded LTQ-FT Ultra, and the LTQ-Orbitrap XL (all Thermo Scientific with Proxeon nano-electrospray ion source).

    Techniques:

    Mass spectra of Fe−8HQ (L) coordination complexes detected in solutions by nano-ESI−MS (nano-electrospray−mass spectrometry); positive ionization mode. The solutions were prepared by mixing of 8-hydroxyquinoline (8HQ) solution with ( a ) Fe II or ( b ) Fe III solutions in molar ratio of metal to ligand of 1:2.

    Journal: International Journal of Molecular Sciences

    Article Title: Antioxidant Properties and the Formation of Iron Coordination Complexes of 8-Hydroxyquinoline

    doi: 10.3390/ijms19123917

    Figure Lengend Snippet: Mass spectra of Fe−8HQ (L) coordination complexes detected in solutions by nano-ESI−MS (nano-electrospray−mass spectrometry); positive ionization mode. The solutions were prepared by mixing of 8-hydroxyquinoline (8HQ) solution with ( a ) Fe II or ( b ) Fe III solutions in molar ratio of metal to ligand of 1:2.

    Article Snippet: Mass Spectrometry Direct infusion nano-electrospray ionization mass spectrometry was carried out in positive ionization mode on a Thermo Electron LTQ-Orbitrap XL mass spectrometer equipped with a nano electrospray ion source (ThermoFisher Scientific, Bremen, Germany) and operated under Xcalibur software 2.2 (ThermoFisher Scientific, Bremen, Germany) as described by Kubicova et al. [ ].

    Techniques: Mass Spectrometry

    Positive ion mode nano-ESI-MS/MS sequencing of permethyl rhFVIIa N -glycans. ( A ) MS/MS product ion profile of the doubly charged doubly sodiated precursor ion at m / z 1227.0913, corresponding to a monosialylated biantennary (6 ppm mass accuracy) N-glycan; ( B ) MS/MS product ion profile of the doubly charged doubly sodiated precursor ion at m / z 1401.1893, corresponding to a monosialylated bifucosylated biantennary N -glycan (1 ppm mass accuracy); ( C ) MS/MS product ion profile of the doubly charged triply sodiated precursor ion at m / z 1076.9753 corresponding to the most intense oligomannose structure, i.e. Man 6 -P-GlcNAc (2 ppm mass accuracy). The glycan representation was made according to the nomenclature of the “Consortium of Functional Glycomics” (CFG).

    Journal: Glycobiology

    Article Title: N-/O-glycosylation analysis of human FVIIa produced in the milk of transgenic rabbits

    doi: 10.1093/glycob/cwt085

    Figure Lengend Snippet: Positive ion mode nano-ESI-MS/MS sequencing of permethyl rhFVIIa N -glycans. ( A ) MS/MS product ion profile of the doubly charged doubly sodiated precursor ion at m / z 1227.0913, corresponding to a monosialylated biantennary (6 ppm mass accuracy) N-glycan; ( B ) MS/MS product ion profile of the doubly charged doubly sodiated precursor ion at m / z 1401.1893, corresponding to a monosialylated bifucosylated biantennary N -glycan (1 ppm mass accuracy); ( C ) MS/MS product ion profile of the doubly charged triply sodiated precursor ion at m / z 1076.9753 corresponding to the most intense oligomannose structure, i.e. Man 6 -P-GlcNAc (2 ppm mass accuracy). The glycan representation was made according to the nomenclature of the “Consortium of Functional Glycomics” (CFG).

    Article Snippet: Nanoelectrospray ionization-tandem mass spectrometry analyses of permethyl oligosaccharides MS analyses of the permethyl N-glycans were performed using a LTQ-Orbitrap hybrid mass spectrometer fitted with a nano-ESI ion source (Thermo Fischer Scientific, Bremen, Germany) under the control of the Tune Plus 2.4 software.

    Techniques: Mass Spectrometry, Sequencing, Functional Assay