Capillary high-performance liquid chromatography/electrospray ion trap time-of-flight mass spectrometry using a novel nanoflow gradient generator

Itô, Shinya; Yoshioka, Shinji; Ogata, Izumi; Yamashita, Eri; Nagai, Shinji; Okumoto, Toyoharu; Ishii, K.; Ito, Masahito; Kaji, Hironori; Takao, Kunihiko; Deguchi, Kisaburo

doi:10.1016/j.chroma.2005.06.096

Cited by 23 publications

(8 citation statements)

References 34 publications

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“…The HPLC/MS system used was a NanoFrontier L (Hitachi High‐Technologies, Tokyo, Japan), which consists of a capillary HPLC system and an ESI‐LIT‐TOF mass spectrometer 23–25. The sample was directly infused into the ESI source through a SilicaTip electrosprayer (tip diameter 10 µm; New Objectives, Woburn, MA, USA).…”

Section: Methodsmentioning

confidence: 99%

Extracellular Silica Nanocoat Confers Thermotolerance on Individual Cells: A Case Study of Material‐Based Functionalization of Living Cells

Wang

Liu

et al. 2010

ChemBioChem

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Section: Methodsmentioning

confidence: 99%

Extracellular Silica Nanocoat Confers Thermotolerance on Individual Cells: A Case Study of Material‐Based Functionalization of Living Cells

Wang

Liu

et al. 2010

ChemBioChem

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“…The HPLC/ESI‐MS instrument used was a NanoFrontier system (Hitachi High‐Technologies, Tokyo, Japan) consisting of a capillary HPLC system based on the AT10PV nanoGR generator36 and an ESI‐IT‐TOF mass spectrometer 37, 38. A Develosil nano‐C30 column (130 µm i.d., 5 mm long; Nomura Chemicals, Aichi, Japan) was used for primary trapping and desalting of the samples.…”

Section: Methodsmentioning

confidence: 99%

Structural assignment of isomeric 2‐aminopyridine‐derivatized monosialylated biantennary N‐linked oligosaccharides using negative‐ion multistage tandem mass spectral matching

Deguchi

Takegawa

Ito

et al. 2005

Rapid Comm Mass Spectrometry

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To investigate the possibility of structural assignment based on negative-ion MS n spectral matching, four isomers of 2-aminopyridine-derivatized (PA) monosialylated oligosaccharides (i.e., complex type N-glycans with an α2-3 or α2-6 linked sialic acid on α1-6 or α1-3 antennae) were analyzed by using high-performance liquid chromatography/electrospray ion trap time-of-flight mass spectrometry (HPLC/ESI-IT-TOF MS). The negative ion [M-2H]2-is observed dominantly in the MS 1 spectra without the loss of a sialic acid. The MS 2 spectra derived from it are sufficiently reproducible that MS 2 spectral matching based on correlation coefficients can be applied to the assignment of these isomers. The isomers containing a sialic acid on α1-6 or α1-3 antennae can be distinguished by MS 2 spectral matching, but the α2-3 and α2-6 linkage types of sialic acid cannot be distinguished by their MS 2 spectra. However, MS 3 spectra derived from fragment ions containing a sialic acid (i.e., C 4 -and D-type ions) clearly differentiate the α2-3 and α2-6 linkage types of sialic acid in their MS 3 spectral patterns.This difference might be rationalized in terms of a proton transfer from the reducing-end mannose to the negatively-charged sialic acid. These two moieties are very close in the structural conformations of the precursor C 4 -type fragment ions, as predicted by molecular mechanics calculations. Thus, negative-ion MS n (n=2, 3) spectral matching was proven to be useful for the structural assignment of these four monosialylated PA N-glycan isomers.3

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“…Experiments on the structural assignment of the O‐glycopeptides were performed using a NanoFrontier L system (Hitachi High‐Technologies, Tokyo, Japan) consisting of a capillary high‐performance liquid chromatography (HPLC) system based on a nanoGR generator46, 47 and a ESI‐LIT TOF mass spectrometer 48. For ECD experiments, we used a modified ESI‐LIT TOF mass spectrometer installed with tandem LITs for CID by He gas and ECD 49.…”

Section: Methodsmentioning

confidence: 99%

Structural analysis of O‐glycopeptides employing negative‐ and positive‐ion multi‐stage mass spectra obtained by collision‐induced and electron‐capture dissociations in linear ion trap time‐of‐flight mass spectrometry

Deguchi

Ito

Baba

et al. 2007

Rapid Comm Mass Spectrometry

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Structural analyses of various glycans attached to proteins and peptides are highly desirable for elucidating their biological roles. An approach based on mass spectrometry (MS) combining both collision-induced dissociation (CID) and electron-capture dissociation (ECD) in the positive- and negative-ion modes has been proposed as a simple and direct method of assigning an O-glycan without releasing it from the peptide and of determining the amino acid sequence of the peptide and glycosylation site. The instrument used is an electrospray ionization (ESI) linear ion trap (LIT) time-of-flight (TOF) mass spectrometer with tandem LITs for CID by He gas and ECD. The proposed approach was tested with two synthetic O-glycopeptides binding a sialyl Lewis x (sLe(x)) oligosaccharide and a 3'-sialyl N-acetyllactosamine (3'-SLN) on a serine (S) residue. In the negative-ion mode, the CID MS(2) spectra of O-glycopeptides showed a relatively abundant glycoside-bond cleavage between the core N-acetylglucosamine (GlcNAc) and serine (S) that yields deprotonated C(3)-type fragment ions of O-glycan and deprotonated Z(0)-type peptide ions. The structure of the sLe(x) (3'-SLN) oligosaccharide was simply assigned by comparing the CID MS(3) spectrum derived from the C(3)-type fragment ion with the CID MS(2) spectra of the sLe(x) and sLe(a) (3'- and 6'-SLN) standards (i.e., negative-ion MS(n) spectral matching). The amino acid sequence of the peptide including the glycosylation site was determined from the ECD MS(2) spectrum in the positive-ion mode.

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Capillary high-performance liquid chromatography/electrospray ion trap time-of-flight mass spectrometry using a novel nanoflow gradient generator

Cited by 23 publications

References 34 publications

Extracellular Silica Nanocoat Confers Thermotolerance on Individual Cells: A Case Study of Material‐Based Functionalization of Living Cells

Extracellular Silica Nanocoat Confers Thermotolerance on Individual Cells: A Case Study of Material‐Based Functionalization of Living Cells

Structural assignment of isomeric 2‐aminopyridine‐derivatized monosialylated biantennary N‐linked oligosaccharides using negative‐ion multistage tandem mass spectral matching

Structural analysis of O‐glycopeptides employing negative‐ and positive‐ion multi‐stage mass spectra obtained by collision‐induced and electron‐capture dissociations in linear ion trap time‐of‐flight mass spectrometry

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