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  • 90
    Agilent technologies hybrid quadrupole time of flight qtof mass spectrometer
    Functional elucidations of a multifunctional and a divergent CYPs ( a ) <t>UPLC-qTOF-MS</t> analysis of the extracts prepared from the yeast expressing OSC , CPR , and each candidate CYP with APCI in positive ion mode. One expected product (red arrows) is generated by CYP87D20 (Cm890, Cl890A, Cl890B, or Cs890). The structure of this product (right) was elucidated by MS/MS and NMR. EIC 441.3727, extracted ion chromatogram of the accurate parent ion at m/z of 441.3727 [M+H] + . ( b ) UPLC-qTOF-MS analysis of the extracts used in ( a ) with ESI in positive mode. One expected product (red arrows) is detected. The structure of this product (right) was elucidated by MS/MS and NMR. EIC 457.3676, extracted ion chromatogram of the accurate parent ion at m/z of 457.3676 [M+H] + . ( c ) UPLC-qTOF-MS analysis of the extracts prepared from the yeast accumulating 11-carbonyl-20 β -hydroxycucurbitadienol and expressing candidate CYPs with ESI in positive ion mode. One expected product peak (red arrow) is generated by CYP81Q59 (Cm180 or Cl180). The structure of this product (below) was elucidated by MS/MS and NMR. EIC 473.3625, extracted ion chromatogram of the accurate parent ion at m/z of 473.3625 [M+H] + .
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    SCIEX qstar hybrid quadrupole time of flight mass spectrometer
    Functional elucidations of a multifunctional and a divergent CYPs ( a ) <t>UPLC-qTOF-MS</t> analysis of the extracts prepared from the yeast expressing OSC , CPR , and each candidate CYP with APCI in positive ion mode. One expected product (red arrows) is generated by CYP87D20 (Cm890, Cl890A, Cl890B, or Cs890). The structure of this product (right) was elucidated by MS/MS and NMR. EIC 441.3727, extracted ion chromatogram of the accurate parent ion at m/z of 441.3727 [M+H] + . ( b ) UPLC-qTOF-MS analysis of the extracts used in ( a ) with ESI in positive mode. One expected product (red arrows) is detected. The structure of this product (right) was elucidated by MS/MS and NMR. EIC 457.3676, extracted ion chromatogram of the accurate parent ion at m/z of 457.3676 [M+H] + . ( c ) UPLC-qTOF-MS analysis of the extracts prepared from the yeast accumulating 11-carbonyl-20 β -hydroxycucurbitadienol and expressing candidate CYPs with ESI in positive ion mode. One expected product peak (red arrow) is generated by CYP81Q59 (Cm180 or Cl180). The structure of this product (below) was elucidated by MS/MS and NMR. EIC 473.3625, extracted ion chromatogram of the accurate parent ion at m/z of 473.3625 [M+H] + .
    Qstar Hybrid Quadrupole Time Of Flight Mass Spectrometer, supplied by SCIEX, used in various techniques. Bioz Stars score: 86/100, based on 32 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    SCIEX hybrid triple quadrupole time of flight mass spectrometer
    Functional elucidations of a multifunctional and a divergent CYPs ( a ) <t>UPLC-qTOF-MS</t> analysis of the extracts prepared from the yeast expressing OSC , CPR , and each candidate CYP with APCI in positive ion mode. One expected product (red arrows) is generated by CYP87D20 (Cm890, Cl890A, Cl890B, or Cs890). The structure of this product (right) was elucidated by MS/MS and NMR. EIC 441.3727, extracted ion chromatogram of the accurate parent ion at m/z of 441.3727 [M+H] + . ( b ) UPLC-qTOF-MS analysis of the extracts used in ( a ) with ESI in positive mode. One expected product (red arrows) is detected. The structure of this product (right) was elucidated by MS/MS and NMR. EIC 457.3676, extracted ion chromatogram of the accurate parent ion at m/z of 457.3676 [M+H] + . ( c ) UPLC-qTOF-MS analysis of the extracts prepared from the yeast accumulating 11-carbonyl-20 β -hydroxycucurbitadienol and expressing candidate CYPs with ESI in positive ion mode. One expected product peak (red arrow) is generated by CYP81Q59 (Cm180 or Cl180). The structure of this product (below) was elucidated by MS/MS and NMR. EIC 473.3625, extracted ion chromatogram of the accurate parent ion at m/z of 473.3625 [M+H] + .
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    SCIEX hybrid quadrupole time of flight tandem mass spectrometer
    ( A ) Xmad2 associates with an 85-kD protein in CSF-arrested extracts. Immunoprecipitation was performed by using a control antibody (lanes 1 and 3 ) or an anti-Xmad2 antibody (lanes 2 and 4 ) as indicated. The immunoprecipitates were washed with a buffer containing 1% Triton X-100 (lanes 1 and 2 ) or 0.1% SDS (lanes 3 and 4 ). The proteins were resolved by SDS-PAGE and stained with Coomassie blue. The migration <t>of</t> p85, IgG, and Xmad2 is indicated on the left, and that of molecular weight standards on the right. ( B ) Sequencing of Xmad1. The unseparated pool of tryptic peptides recovered from the gel matrix was analyzed using a novel <t>quadrupole</t> TOF <t>mass</t> <t>spectrometer.</t> ( a ) Mass spectrum of the unseparated tryptic digest of the Xmad1 band. The peptide ions designated with T were in turn isolated by a quadrupole mass analyzer, fragmented in the collision cell, and then their <t>tandem</t> mass spectra were acquired with a reflector <t>time-of-flight</t> module. Peaks designated with asterisks are trypsin autolysis products. The peptide ion designated with A belongs to the antibody used in the purification of Xmad1. ( b ) Tandem mass spectrum of the doubly charged peptide ion T 8 (marked with an arrow in a ). Upon collisional fragmentation, tryptic peptides tend to produce a continuous series of fragment ions containing the COOH terminus (Y″ ions; Roepstorff and Fohlman, 1984). The peptide sequence (shown above) is deduced by considering precise mass differences between adjacent Y″ ions. M *, N -acetylated methionine sulfoxide amino acid residue. The spectrum also contains minor series of the NH 2 -terminal fragment ions (B ions) as well as internal fragment ions. Therefore to deduce the sequence with high confidence it is necessary to distinguish Y″ ions from the other ions in the spectrum. This has been achieved by selective isotopic labeling of the COOH-terminal carboxyl group of the peptides. ( c ) A zoom of the region in the tandem mass spectrum of T 8 shows the principal of sequence readout of isotopically labeled peptides. Upon tryptic cleavage of the protein in a buffer containing H 2 16 O/H 2 18 O 1:1 (vol/vol) COOH-terminal carboxyl groups of peptide molecules incorporate 16 O and 18 O atoms in a 1:1 ratio. Thus the fragment ions containing the COOH terminus of the peptide (mostly Y″ ions) appear in the fragment spectrum as a characteristic isotopic pattern—a doublet split by 2 D. B ions or other fragment ions not containing COOH-terminal carboxyl group are observed as ions having normal isotopic pattern.
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    SCIEX qstarxl hybrid quadrupole time of flight mass spectrometer
    ( A ) Xmad2 associates with an 85-kD protein in CSF-arrested extracts. Immunoprecipitation was performed by using a control antibody (lanes 1 and 3 ) or an anti-Xmad2 antibody (lanes 2 and 4 ) as indicated. The immunoprecipitates were washed with a buffer containing 1% Triton X-100 (lanes 1 and 2 ) or 0.1% SDS (lanes 3 and 4 ). The proteins were resolved by SDS-PAGE and stained with Coomassie blue. The migration <t>of</t> p85, IgG, and Xmad2 is indicated on the left, and that of molecular weight standards on the right. ( B ) Sequencing of Xmad1. The unseparated pool of tryptic peptides recovered from the gel matrix was analyzed using a novel <t>quadrupole</t> TOF <t>mass</t> <t>spectrometer.</t> ( a ) Mass spectrum of the unseparated tryptic digest of the Xmad1 band. The peptide ions designated with T were in turn isolated by a quadrupole mass analyzer, fragmented in the collision cell, and then their <t>tandem</t> mass spectra were acquired with a reflector <t>time-of-flight</t> module. Peaks designated with asterisks are trypsin autolysis products. The peptide ion designated with A belongs to the antibody used in the purification of Xmad1. ( b ) Tandem mass spectrum of the doubly charged peptide ion T 8 (marked with an arrow in a ). Upon collisional fragmentation, tryptic peptides tend to produce a continuous series of fragment ions containing the COOH terminus (Y″ ions; Roepstorff and Fohlman, 1984). The peptide sequence (shown above) is deduced by considering precise mass differences between adjacent Y″ ions. M *, N -acetylated methionine sulfoxide amino acid residue. The spectrum also contains minor series of the NH 2 -terminal fragment ions (B ions) as well as internal fragment ions. Therefore to deduce the sequence with high confidence it is necessary to distinguish Y″ ions from the other ions in the spectrum. This has been achieved by selective isotopic labeling of the COOH-terminal carboxyl group of the peptides. ( c ) A zoom of the region in the tandem mass spectrum of T 8 shows the principal of sequence readout of isotopically labeled peptides. Upon tryptic cleavage of the protein in a buffer containing H 2 16 O/H 2 18 O 1:1 (vol/vol) COOH-terminal carboxyl groups of peptide molecules incorporate 16 O and 18 O atoms in a 1:1 ratio. Thus the fragment ions containing the COOH terminus of the peptide (mostly Y″ ions) appear in the fragment spectrum as a characteristic isotopic pattern—a doublet split by 2 D. B ions or other fragment ions not containing COOH-terminal carboxyl group are observed as ions having normal isotopic pattern.
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    Bruker Corporation hybrid quadrupole time of flight qtof mass spectrometer mass spectrometer ms
    ( A ) Xmad2 associates with an 85-kD protein in CSF-arrested extracts. Immunoprecipitation was performed by using a control antibody (lanes 1 and 3 ) or an anti-Xmad2 antibody (lanes 2 and 4 ) as indicated. The immunoprecipitates were washed with a buffer containing 1% Triton X-100 (lanes 1 and 2 ) or 0.1% SDS (lanes 3 and 4 ). The proteins were resolved by SDS-PAGE and stained with Coomassie blue. The migration <t>of</t> p85, IgG, and Xmad2 is indicated on the left, and that of molecular weight standards on the right. ( B ) Sequencing of Xmad1. The unseparated pool of tryptic peptides recovered from the gel matrix was analyzed using a novel <t>quadrupole</t> TOF <t>mass</t> <t>spectrometer.</t> ( a ) Mass spectrum of the unseparated tryptic digest of the Xmad1 band. The peptide ions designated with T were in turn isolated by a quadrupole mass analyzer, fragmented in the collision cell, and then their <t>tandem</t> mass spectra were acquired with a reflector <t>time-of-flight</t> module. Peaks designated with asterisks are trypsin autolysis products. The peptide ion designated with A belongs to the antibody used in the purification of Xmad1. ( b ) Tandem mass spectrum of the doubly charged peptide ion T 8 (marked with an arrow in a ). Upon collisional fragmentation, tryptic peptides tend to produce a continuous series of fragment ions containing the COOH terminus (Y″ ions; Roepstorff and Fohlman, 1984). The peptide sequence (shown above) is deduced by considering precise mass differences between adjacent Y″ ions. M *, N -acetylated methionine sulfoxide amino acid residue. The spectrum also contains minor series of the NH 2 -terminal fragment ions (B ions) as well as internal fragment ions. Therefore to deduce the sequence with high confidence it is necessary to distinguish Y″ ions from the other ions in the spectrum. This has been achieved by selective isotopic labeling of the COOH-terminal carboxyl group of the peptides. ( c ) A zoom of the region in the tandem mass spectrum of T 8 shows the principal of sequence readout of isotopically labeled peptides. Upon tryptic cleavage of the protein in a buffer containing H 2 16 O/H 2 18 O 1:1 (vol/vol) COOH-terminal carboxyl groups of peptide molecules incorporate 16 O and 18 O atoms in a 1:1 ratio. Thus the fragment ions containing the COOH terminus of the peptide (mostly Y″ ions) appear in the fragment spectrum as a characteristic isotopic pattern—a doublet split by 2 D. B ions or other fragment ions not containing COOH-terminal carboxyl group are observed as ions having normal isotopic pattern.
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    Waters Corporation hybrid quadrupole time of flight q tof mass spectrometer
    ( A ) Xmad2 associates with an 85-kD protein in CSF-arrested extracts. Immunoprecipitation was performed by using a control antibody (lanes 1 and 3 ) or an anti-Xmad2 antibody (lanes 2 and 4 ) as indicated. The immunoprecipitates were washed with a buffer containing 1% Triton X-100 (lanes 1 and 2 ) or 0.1% SDS (lanes 3 and 4 ). The proteins were resolved by SDS-PAGE and stained with Coomassie blue. The migration <t>of</t> p85, IgG, and Xmad2 is indicated on the left, and that of molecular weight standards on the right. ( B ) Sequencing of Xmad1. The unseparated pool of tryptic peptides recovered from the gel matrix was analyzed using a novel <t>quadrupole</t> TOF <t>mass</t> <t>spectrometer.</t> ( a ) Mass spectrum of the unseparated tryptic digest of the Xmad1 band. The peptide ions designated with T were in turn isolated by a quadrupole mass analyzer, fragmented in the collision cell, and then their <t>tandem</t> mass spectra were acquired with a reflector <t>time-of-flight</t> module. Peaks designated with asterisks are trypsin autolysis products. The peptide ion designated with A belongs to the antibody used in the purification of Xmad1. ( b ) Tandem mass spectrum of the doubly charged peptide ion T 8 (marked with an arrow in a ). Upon collisional fragmentation, tryptic peptides tend to produce a continuous series of fragment ions containing the COOH terminus (Y″ ions; Roepstorff and Fohlman, 1984). The peptide sequence (shown above) is deduced by considering precise mass differences between adjacent Y″ ions. M *, N -acetylated methionine sulfoxide amino acid residue. The spectrum also contains minor series of the NH 2 -terminal fragment ions (B ions) as well as internal fragment ions. Therefore to deduce the sequence with high confidence it is necessary to distinguish Y″ ions from the other ions in the spectrum. This has been achieved by selective isotopic labeling of the COOH-terminal carboxyl group of the peptides. ( c ) A zoom of the region in the tandem mass spectrum of T 8 shows the principal of sequence readout of isotopically labeled peptides. Upon tryptic cleavage of the protein in a buffer containing H 2 16 O/H 2 18 O 1:1 (vol/vol) COOH-terminal carboxyl groups of peptide molecules incorporate 16 O and 18 O atoms in a 1:1 ratio. Thus the fragment ions containing the COOH terminus of the peptide (mostly Y″ ions) appear in the fragment spectrum as a characteristic isotopic pattern—a doublet split by 2 D. B ions or other fragment ions not containing COOH-terminal carboxyl group are observed as ions having normal isotopic pattern.
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    SCIEX qstar elite hybrid quadrupole time of flight mass spectrometer
    ( A ) Xmad2 associates with an 85-kD protein in CSF-arrested extracts. Immunoprecipitation was performed by using a control antibody (lanes 1 and 3 ) or an anti-Xmad2 antibody (lanes 2 and 4 ) as indicated. The immunoprecipitates were washed with a buffer containing 1% Triton X-100 (lanes 1 and 2 ) or 0.1% SDS (lanes 3 and 4 ). The proteins were resolved by SDS-PAGE and stained with Coomassie blue. The migration <t>of</t> p85, IgG, and Xmad2 is indicated on the left, and that of molecular weight standards on the right. ( B ) Sequencing of Xmad1. The unseparated pool of tryptic peptides recovered from the gel matrix was analyzed using a novel <t>quadrupole</t> TOF <t>mass</t> <t>spectrometer.</t> ( a ) Mass spectrum of the unseparated tryptic digest of the Xmad1 band. The peptide ions designated with T were in turn isolated by a quadrupole mass analyzer, fragmented in the collision cell, and then their <t>tandem</t> mass spectra were acquired with a reflector <t>time-of-flight</t> module. Peaks designated with asterisks are trypsin autolysis products. The peptide ion designated with A belongs to the antibody used in the purification of Xmad1. ( b ) Tandem mass spectrum of the doubly charged peptide ion T 8 (marked with an arrow in a ). Upon collisional fragmentation, tryptic peptides tend to produce a continuous series of fragment ions containing the COOH terminus (Y″ ions; Roepstorff and Fohlman, 1984). The peptide sequence (shown above) is deduced by considering precise mass differences between adjacent Y″ ions. M *, N -acetylated methionine sulfoxide amino acid residue. The spectrum also contains minor series of the NH 2 -terminal fragment ions (B ions) as well as internal fragment ions. Therefore to deduce the sequence with high confidence it is necessary to distinguish Y″ ions from the other ions in the spectrum. This has been achieved by selective isotopic labeling of the COOH-terminal carboxyl group of the peptides. ( c ) A zoom of the region in the tandem mass spectrum of T 8 shows the principal of sequence readout of isotopically labeled peptides. Upon tryptic cleavage of the protein in a buffer containing H 2 16 O/H 2 18 O 1:1 (vol/vol) COOH-terminal carboxyl groups of peptide molecules incorporate 16 O and 18 O atoms in a 1:1 ratio. Thus the fragment ions containing the COOH terminus of the peptide (mostly Y″ ions) appear in the fragment spectrum as a characteristic isotopic pattern—a doublet split by 2 D. B ions or other fragment ions not containing COOH-terminal carboxyl group are observed as ions having normal isotopic pattern.
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    Waters Corporation qtof ultima hybrid quadrupole time of flight mass spectrometer
    ( A ) Xmad2 associates with an 85-kD protein in CSF-arrested extracts. Immunoprecipitation was performed by using a control antibody (lanes 1 and 3 ) or an anti-Xmad2 antibody (lanes 2 and 4 ) as indicated. The immunoprecipitates were washed with a buffer containing 1% Triton X-100 (lanes 1 and 2 ) or 0.1% SDS (lanes 3 and 4 ). The proteins were resolved by SDS-PAGE and stained with Coomassie blue. The migration <t>of</t> p85, IgG, and Xmad2 is indicated on the left, and that of molecular weight standards on the right. ( B ) Sequencing of Xmad1. The unseparated pool of tryptic peptides recovered from the gel matrix was analyzed using a novel <t>quadrupole</t> TOF <t>mass</t> <t>spectrometer.</t> ( a ) Mass spectrum of the unseparated tryptic digest of the Xmad1 band. The peptide ions designated with T were in turn isolated by a quadrupole mass analyzer, fragmented in the collision cell, and then their <t>tandem</t> mass spectra were acquired with a reflector <t>time-of-flight</t> module. Peaks designated with asterisks are trypsin autolysis products. The peptide ion designated with A belongs to the antibody used in the purification of Xmad1. ( b ) Tandem mass spectrum of the doubly charged peptide ion T 8 (marked with an arrow in a ). Upon collisional fragmentation, tryptic peptides tend to produce a continuous series of fragment ions containing the COOH terminus (Y″ ions; Roepstorff and Fohlman, 1984). The peptide sequence (shown above) is deduced by considering precise mass differences between adjacent Y″ ions. M *, N -acetylated methionine sulfoxide amino acid residue. The spectrum also contains minor series of the NH 2 -terminal fragment ions (B ions) as well as internal fragment ions. Therefore to deduce the sequence with high confidence it is necessary to distinguish Y″ ions from the other ions in the spectrum. This has been achieved by selective isotopic labeling of the COOH-terminal carboxyl group of the peptides. ( c ) A zoom of the region in the tandem mass spectrum of T 8 shows the principal of sequence readout of isotopically labeled peptides. Upon tryptic cleavage of the protein in a buffer containing H 2 16 O/H 2 18 O 1:1 (vol/vol) COOH-terminal carboxyl groups of peptide molecules incorporate 16 O and 18 O atoms in a 1:1 ratio. Thus the fragment ions containing the COOH terminus of the peptide (mostly Y″ ions) appear in the fragment spectrum as a characteristic isotopic pattern—a doublet split by 2 D. B ions or other fragment ions not containing COOH-terminal carboxyl group are observed as ions having normal isotopic pattern.
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    Waters Corporation quadrupole time of flight qtof micro hybrid mass spectrometer
    ( A ) Xmad2 associates with an 85-kD protein in CSF-arrested extracts. Immunoprecipitation was performed by using a control antibody (lanes 1 and 3 ) or an anti-Xmad2 antibody (lanes 2 and 4 ) as indicated. The immunoprecipitates were washed with a buffer containing 1% Triton X-100 (lanes 1 and 2 ) or 0.1% SDS (lanes 3 and 4 ). The proteins were resolved by SDS-PAGE and stained with Coomassie blue. The migration <t>of</t> p85, IgG, and Xmad2 is indicated on the left, and that of molecular weight standards on the right. ( B ) Sequencing of Xmad1. The unseparated pool of tryptic peptides recovered from the gel matrix was analyzed using a novel <t>quadrupole</t> TOF <t>mass</t> <t>spectrometer.</t> ( a ) Mass spectrum of the unseparated tryptic digest of the Xmad1 band. The peptide ions designated with T were in turn isolated by a quadrupole mass analyzer, fragmented in the collision cell, and then their <t>tandem</t> mass spectra were acquired with a reflector <t>time-of-flight</t> module. Peaks designated with asterisks are trypsin autolysis products. The peptide ion designated with A belongs to the antibody used in the purification of Xmad1. ( b ) Tandem mass spectrum of the doubly charged peptide ion T 8 (marked with an arrow in a ). Upon collisional fragmentation, tryptic peptides tend to produce a continuous series of fragment ions containing the COOH terminus (Y″ ions; Roepstorff and Fohlman, 1984). The peptide sequence (shown above) is deduced by considering precise mass differences between adjacent Y″ ions. M *, N -acetylated methionine sulfoxide amino acid residue. The spectrum also contains minor series of the NH 2 -terminal fragment ions (B ions) as well as internal fragment ions. Therefore to deduce the sequence with high confidence it is necessary to distinguish Y″ ions from the other ions in the spectrum. This has been achieved by selective isotopic labeling of the COOH-terminal carboxyl group of the peptides. ( c ) A zoom of the region in the tandem mass spectrum of T 8 shows the principal of sequence readout of isotopically labeled peptides. Upon tryptic cleavage of the protein in a buffer containing H 2 16 O/H 2 18 O 1:1 (vol/vol) COOH-terminal carboxyl groups of peptide molecules incorporate 16 O and 18 O atoms in a 1:1 ratio. Thus the fragment ions containing the COOH terminus of the peptide (mostly Y″ ions) appear in the fragment spectrum as a characteristic isotopic pattern—a doublet split by 2 D. B ions or other fragment ions not containing COOH-terminal carboxyl group are observed as ions having normal isotopic pattern.
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    Bruker Corporation microtof q hybrid quadrupole time of flight mass spectrometer
    ( A ) Xmad2 associates with an 85-kD protein in CSF-arrested extracts. Immunoprecipitation was performed by using a control antibody (lanes 1 and 3 ) or an anti-Xmad2 antibody (lanes 2 and 4 ) as indicated. The immunoprecipitates were washed with a buffer containing 1% Triton X-100 (lanes 1 and 2 ) or 0.1% SDS (lanes 3 and 4 ). The proteins were resolved by SDS-PAGE and stained with Coomassie blue. The migration <t>of</t> p85, IgG, and Xmad2 is indicated on the left, and that of molecular weight standards on the right. ( B ) Sequencing of Xmad1. The unseparated pool of tryptic peptides recovered from the gel matrix was analyzed using a novel <t>quadrupole</t> TOF <t>mass</t> <t>spectrometer.</t> ( a ) Mass spectrum of the unseparated tryptic digest of the Xmad1 band. The peptide ions designated with T were in turn isolated by a quadrupole mass analyzer, fragmented in the collision cell, and then their <t>tandem</t> mass spectra were acquired with a reflector <t>time-of-flight</t> module. Peaks designated with asterisks are trypsin autolysis products. The peptide ion designated with A belongs to the antibody used in the purification of Xmad1. ( b ) Tandem mass spectrum of the doubly charged peptide ion T 8 (marked with an arrow in a ). Upon collisional fragmentation, tryptic peptides tend to produce a continuous series of fragment ions containing the COOH terminus (Y″ ions; Roepstorff and Fohlman, 1984). The peptide sequence (shown above) is deduced by considering precise mass differences between adjacent Y″ ions. M *, N -acetylated methionine sulfoxide amino acid residue. The spectrum also contains minor series of the NH 2 -terminal fragment ions (B ions) as well as internal fragment ions. Therefore to deduce the sequence with high confidence it is necessary to distinguish Y″ ions from the other ions in the spectrum. This has been achieved by selective isotopic labeling of the COOH-terminal carboxyl group of the peptides. ( c ) A zoom of the region in the tandem mass spectrum of T 8 shows the principal of sequence readout of isotopically labeled peptides. Upon tryptic cleavage of the protein in a buffer containing H 2 16 O/H 2 18 O 1:1 (vol/vol) COOH-terminal carboxyl groups of peptide molecules incorporate 16 O and 18 O atoms in a 1:1 ratio. Thus the fragment ions containing the COOH terminus of the peptide (mostly Y″ ions) appear in the fragment spectrum as a characteristic isotopic pattern—a doublet split by 2 D. B ions or other fragment ions not containing COOH-terminal carboxyl group are observed as ions having normal isotopic pattern.
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    ( A ) Xmad2 associates with an 85-kD protein in CSF-arrested extracts. Immunoprecipitation was performed by using a control antibody (lanes 1 and 3 ) or an anti-Xmad2 antibody (lanes 2 and 4 ) as indicated. The immunoprecipitates were washed with a buffer containing 1% Triton X-100 (lanes 1 and 2 ) or 0.1% SDS (lanes 3 and 4 ). The proteins were resolved by SDS-PAGE and stained with Coomassie blue. The migration <t>of</t> p85, IgG, and Xmad2 is indicated on the left, and that of molecular weight standards on the right. ( B ) Sequencing of Xmad1. The unseparated pool of tryptic peptides recovered from the gel matrix was analyzed using a novel <t>quadrupole</t> TOF <t>mass</t> <t>spectrometer.</t> ( a ) Mass spectrum of the unseparated tryptic digest of the Xmad1 band. The peptide ions designated with T were in turn isolated by a quadrupole mass analyzer, fragmented in the collision cell, and then their <t>tandem</t> mass spectra were acquired with a reflector <t>time-of-flight</t> module. Peaks designated with asterisks are trypsin autolysis products. The peptide ion designated with A belongs to the antibody used in the purification of Xmad1. ( b ) Tandem mass spectrum of the doubly charged peptide ion T 8 (marked with an arrow in a ). Upon collisional fragmentation, tryptic peptides tend to produce a continuous series of fragment ions containing the COOH terminus (Y″ ions; Roepstorff and Fohlman, 1984). The peptide sequence (shown above) is deduced by considering precise mass differences between adjacent Y″ ions. M *, N -acetylated methionine sulfoxide amino acid residue. The spectrum also contains minor series of the NH 2 -terminal fragment ions (B ions) as well as internal fragment ions. Therefore to deduce the sequence with high confidence it is necessary to distinguish Y″ ions from the other ions in the spectrum. This has been achieved by selective isotopic labeling of the COOH-terminal carboxyl group of the peptides. ( c ) A zoom of the region in the tandem mass spectrum of T 8 shows the principal of sequence readout of isotopically labeled peptides. Upon tryptic cleavage of the protein in a buffer containing H 2 16 O/H 2 18 O 1:1 (vol/vol) COOH-terminal carboxyl groups of peptide molecules incorporate 16 O and 18 O atoms in a 1:1 ratio. Thus the fragment ions containing the COOH terminus of the peptide (mostly Y″ ions) appear in the fragment spectrum as a characteristic isotopic pattern—a doublet split by 2 D. B ions or other fragment ions not containing COOH-terminal carboxyl group are observed as ions having normal isotopic pattern.
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    Nonaqueous ESI-MS analysis of pilin protein. (A) Mass spectrum of the intact protein sample acquired on the <t>Q-TOF2</t> mass spectrometer. The molecular mass profile derived from this mass spectrum is presented in the inset. (B) Top-down MS/MS spectrum of
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    Nonaqueous ESI-MS analysis of pilin protein. (A) Mass spectrum of the intact protein sample acquired on the <t>Q-TOF2</t> mass spectrometer. The molecular mass profile derived from this mass spectrum is presented in the inset. (B) Top-down MS/MS spectrum of
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    Nonaqueous ESI-MS analysis of pilin protein. (A) Mass spectrum of the intact protein sample acquired on the <t>Q-TOF2</t> mass spectrometer. The molecular mass profile derived from this mass spectrum is presented in the inset. (B) Top-down MS/MS spectrum of
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    <t>Hybrid</t> <t>quadrupole</t> <t>orthogonal</t> <t>time-of-flight</t> <t>mass</t> spectrometry (Q-TOF) detects PIB and eight other monoacylphloroglucinols
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    Identification <t>of</t> ions from MALDI TIMS by precursor ion fragmentation and product ion scan . A thin section from the ovarian tumor in Fig. 3 was analyzed using a <t>hybrid</t> <t>quadrupole</t> <t>time-of-flight</t> <t>mass</t> <t>spectrometer</t> (ABI Q-STAR) in negative ionization mode with selection of the shown parent ions for fragmentation and analysis of the product ion spectra. (A and B) Product ion spectrum for each compound ( m/z 778.6 ion was identified as a d18:1/C16:0 ceramide monohexosylsulfatide and m/z 885.6 was most consistent with the shown phosphatidylinositol).
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    Identification <t>of</t> ions from MALDI TIMS by precursor ion fragmentation and product ion scan . A thin section from the ovarian tumor in Fig. 3 was analyzed using a <t>hybrid</t> <t>quadrupole</t> <t>time-of-flight</t> <t>mass</t> <t>spectrometer</t> (ABI Q-STAR) in negative ionization mode with selection of the shown parent ions for fragmentation and analysis of the product ion spectra. (A and B) Product ion spectrum for each compound ( m/z 778.6 ion was identified as a d18:1/C16:0 ceramide monohexosylsulfatide and m/z 885.6 was most consistent with the shown phosphatidylinositol).
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    Identification <t>of</t> ions from MALDI TIMS by precursor ion fragmentation and product ion scan . A thin section from the ovarian tumor in Fig. 3 was analyzed using a <t>hybrid</t> <t>quadrupole</t> <t>time-of-flight</t> <t>mass</t> <t>spectrometer</t> (ABI Q-STAR) in negative ionization mode with selection of the shown parent ions for fragmentation and analysis of the product ion spectra. (A and B) Product ion spectrum for each compound ( m/z 778.6 ion was identified as a d18:1/C16:0 ceramide monohexosylsulfatide and m/z 885.6 was most consistent with the shown phosphatidylinositol).
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    Identification <t>of</t> ions from MALDI TIMS by precursor ion fragmentation and product ion scan . A thin section from the ovarian tumor in Fig. 3 was analyzed using a <t>hybrid</t> <t>quadrupole</t> <t>time-of-flight</t> <t>mass</t> <t>spectrometer</t> (ABI Q-STAR) in negative ionization mode with selection of the shown parent ions for fragmentation and analysis of the product ion spectra. (A and B) Product ion spectrum for each compound ( m/z 778.6 ion was identified as a d18:1/C16:0 ceramide monohexosylsulfatide and m/z 885.6 was most consistent with the shown phosphatidylinositol).
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    Identification <t>of</t> ions from MALDI TIMS by precursor ion fragmentation and product ion scan . A thin section from the ovarian tumor in Fig. 3 was analyzed using a <t>hybrid</t> <t>quadrupole</t> <t>time-of-flight</t> <t>mass</t> <t>spectrometer</t> (ABI Q-STAR) in negative ionization mode with selection of the shown parent ions for fragmentation and analysis of the product ion spectra. (A and B) Product ion spectrum for each compound ( m/z 778.6 ion was identified as a d18:1/C16:0 ceramide monohexosylsulfatide and m/z 885.6 was most consistent with the shown phosphatidylinositol).
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    Image Search Results


    Functional elucidations of a multifunctional and a divergent CYPs ( a ) UPLC-qTOF-MS analysis of the extracts prepared from the yeast expressing OSC , CPR , and each candidate CYP with APCI in positive ion mode. One expected product (red arrows) is generated by CYP87D20 (Cm890, Cl890A, Cl890B, or Cs890). The structure of this product (right) was elucidated by MS/MS and NMR. EIC 441.3727, extracted ion chromatogram of the accurate parent ion at m/z of 441.3727 [M+H] + . ( b ) UPLC-qTOF-MS analysis of the extracts used in ( a ) with ESI in positive mode. One expected product (red arrows) is detected. The structure of this product (right) was elucidated by MS/MS and NMR. EIC 457.3676, extracted ion chromatogram of the accurate parent ion at m/z of 457.3676 [M+H] + . ( c ) UPLC-qTOF-MS analysis of the extracts prepared from the yeast accumulating 11-carbonyl-20 β -hydroxycucurbitadienol and expressing candidate CYPs with ESI in positive ion mode. One expected product peak (red arrow) is generated by CYP81Q59 (Cm180 or Cl180). The structure of this product (below) was elucidated by MS/MS and NMR. EIC 473.3625, extracted ion chromatogram of the accurate parent ion at m/z of 473.3625 [M+H] + .

    Journal: Nature plants

    Article Title: Convergence and divergence of cucurbitacin biosynthesis and regulation in Cucurbitaceae

    doi: 10.1038/nplants.2016.183

    Figure Lengend Snippet: Functional elucidations of a multifunctional and a divergent CYPs ( a ) UPLC-qTOF-MS analysis of the extracts prepared from the yeast expressing OSC , CPR , and each candidate CYP with APCI in positive ion mode. One expected product (red arrows) is generated by CYP87D20 (Cm890, Cl890A, Cl890B, or Cs890). The structure of this product (right) was elucidated by MS/MS and NMR. EIC 441.3727, extracted ion chromatogram of the accurate parent ion at m/z of 441.3727 [M+H] + . ( b ) UPLC-qTOF-MS analysis of the extracts used in ( a ) with ESI in positive mode. One expected product (red arrows) is detected. The structure of this product (right) was elucidated by MS/MS and NMR. EIC 457.3676, extracted ion chromatogram of the accurate parent ion at m/z of 457.3676 [M+H] + . ( c ) UPLC-qTOF-MS analysis of the extracts prepared from the yeast accumulating 11-carbonyl-20 β -hydroxycucurbitadienol and expressing candidate CYPs with ESI in positive ion mode. One expected product peak (red arrow) is generated by CYP81Q59 (Cm180 or Cl180). The structure of this product (below) was elucidated by MS/MS and NMR. EIC 473.3625, extracted ion chromatogram of the accurate parent ion at m/z of 473.3625 [M+H] + .

    Article Snippet: The UPLC was coupled with an electrospray ionization (ESI), a hybrid quadrupole time-of-flight (qTOF) mass spectrometer (model 6540, Agilent).

    Techniques: Functional Assay, Mass Spectrometry, Expressing, Generated, Nuclear Magnetic Resonance

    Elucidation of the catalytic steps invovled in CuB and CuE biosynthesis ( a ) GC-MS profiles of the extracts prepared from the yeast that harbored CmBi , ClBi , or empty vector, and an authentic cucurbitadienol standard. EI + , electron ionization in positive ion mode; TIC, total ion chromatograms; EIC 134, extracted ion chromatograms of the characteristic fragment ion of cucurbitadienol at a mass/charge ratio ( m/z ) of 134. ( b and c ) UPLC-qTOF-MS analysis of the ACT-catalytic reaction products. The sample without CmACT or ClACT protein was served as the negative control. EIC 576.3531 and 574.3374, extracted ion chromatograms of the accurate parent ions at m/z ] + ] + , for CuB and CuE, respectively.

    Journal: Nature plants

    Article Title: Convergence and divergence of cucurbitacin biosynthesis and regulation in Cucurbitaceae

    doi: 10.1038/nplants.2016.183

    Figure Lengend Snippet: Elucidation of the catalytic steps invovled in CuB and CuE biosynthesis ( a ) GC-MS profiles of the extracts prepared from the yeast that harbored CmBi , ClBi , or empty vector, and an authentic cucurbitadienol standard. EI + , electron ionization in positive ion mode; TIC, total ion chromatograms; EIC 134, extracted ion chromatograms of the characteristic fragment ion of cucurbitadienol at a mass/charge ratio ( m/z ) of 134. ( b and c ) UPLC-qTOF-MS analysis of the ACT-catalytic reaction products. The sample without CmACT or ClACT protein was served as the negative control. EIC 576.3531 and 574.3374, extracted ion chromatograms of the accurate parent ions at m/z ] + ] + , for CuB and CuE, respectively.

    Article Snippet: The UPLC was coupled with an electrospray ionization (ESI), a hybrid quadrupole time-of-flight (qTOF) mass spectrometer (model 6540, Agilent).

    Techniques: Gas Chromatography-Mass Spectrometry, Plasmid Preparation, Mass Spectrometry, Activated Clotting Time Assay, Negative Control

    ( A ) Xmad2 associates with an 85-kD protein in CSF-arrested extracts. Immunoprecipitation was performed by using a control antibody (lanes 1 and 3 ) or an anti-Xmad2 antibody (lanes 2 and 4 ) as indicated. The immunoprecipitates were washed with a buffer containing 1% Triton X-100 (lanes 1 and 2 ) or 0.1% SDS (lanes 3 and 4 ). The proteins were resolved by SDS-PAGE and stained with Coomassie blue. The migration of p85, IgG, and Xmad2 is indicated on the left, and that of molecular weight standards on the right. ( B ) Sequencing of Xmad1. The unseparated pool of tryptic peptides recovered from the gel matrix was analyzed using a novel quadrupole TOF mass spectrometer. ( a ) Mass spectrum of the unseparated tryptic digest of the Xmad1 band. The peptide ions designated with T were in turn isolated by a quadrupole mass analyzer, fragmented in the collision cell, and then their tandem mass spectra were acquired with a reflector time-of-flight module. Peaks designated with asterisks are trypsin autolysis products. The peptide ion designated with A belongs to the antibody used in the purification of Xmad1. ( b ) Tandem mass spectrum of the doubly charged peptide ion T 8 (marked with an arrow in a ). Upon collisional fragmentation, tryptic peptides tend to produce a continuous series of fragment ions containing the COOH terminus (Y″ ions; Roepstorff and Fohlman, 1984). The peptide sequence (shown above) is deduced by considering precise mass differences between adjacent Y″ ions. M *, N -acetylated methionine sulfoxide amino acid residue. The spectrum also contains minor series of the NH 2 -terminal fragment ions (B ions) as well as internal fragment ions. Therefore to deduce the sequence with high confidence it is necessary to distinguish Y″ ions from the other ions in the spectrum. This has been achieved by selective isotopic labeling of the COOH-terminal carboxyl group of the peptides. ( c ) A zoom of the region in the tandem mass spectrum of T 8 shows the principal of sequence readout of isotopically labeled peptides. Upon tryptic cleavage of the protein in a buffer containing H 2 16 O/H 2 18 O 1:1 (vol/vol) COOH-terminal carboxyl groups of peptide molecules incorporate 16 O and 18 O atoms in a 1:1 ratio. Thus the fragment ions containing the COOH terminus of the peptide (mostly Y″ ions) appear in the fragment spectrum as a characteristic isotopic pattern—a doublet split by 2 D. B ions or other fragment ions not containing COOH-terminal carboxyl group are observed as ions having normal isotopic pattern.

    Journal: The Journal of Cell Biology

    Article Title: Spindle Checkpoint Protein Xmad1 Recruits Xmad2 to Unattached Kinetochores

    doi:

    Figure Lengend Snippet: ( A ) Xmad2 associates with an 85-kD protein in CSF-arrested extracts. Immunoprecipitation was performed by using a control antibody (lanes 1 and 3 ) or an anti-Xmad2 antibody (lanes 2 and 4 ) as indicated. The immunoprecipitates were washed with a buffer containing 1% Triton X-100 (lanes 1 and 2 ) or 0.1% SDS (lanes 3 and 4 ). The proteins were resolved by SDS-PAGE and stained with Coomassie blue. The migration of p85, IgG, and Xmad2 is indicated on the left, and that of molecular weight standards on the right. ( B ) Sequencing of Xmad1. The unseparated pool of tryptic peptides recovered from the gel matrix was analyzed using a novel quadrupole TOF mass spectrometer. ( a ) Mass spectrum of the unseparated tryptic digest of the Xmad1 band. The peptide ions designated with T were in turn isolated by a quadrupole mass analyzer, fragmented in the collision cell, and then their tandem mass spectra were acquired with a reflector time-of-flight module. Peaks designated with asterisks are trypsin autolysis products. The peptide ion designated with A belongs to the antibody used in the purification of Xmad1. ( b ) Tandem mass spectrum of the doubly charged peptide ion T 8 (marked with an arrow in a ). Upon collisional fragmentation, tryptic peptides tend to produce a continuous series of fragment ions containing the COOH terminus (Y″ ions; Roepstorff and Fohlman, 1984). The peptide sequence (shown above) is deduced by considering precise mass differences between adjacent Y″ ions. M *, N -acetylated methionine sulfoxide amino acid residue. The spectrum also contains minor series of the NH 2 -terminal fragment ions (B ions) as well as internal fragment ions. Therefore to deduce the sequence with high confidence it is necessary to distinguish Y″ ions from the other ions in the spectrum. This has been achieved by selective isotopic labeling of the COOH-terminal carboxyl group of the peptides. ( c ) A zoom of the region in the tandem mass spectrum of T 8 shows the principal of sequence readout of isotopically labeled peptides. Upon tryptic cleavage of the protein in a buffer containing H 2 16 O/H 2 18 O 1:1 (vol/vol) COOH-terminal carboxyl groups of peptide molecules incorporate 16 O and 18 O atoms in a 1:1 ratio. Thus the fragment ions containing the COOH terminus of the peptide (mostly Y″ ions) appear in the fragment spectrum as a characteristic isotopic pattern—a doublet split by 2 D. B ions or other fragment ions not containing COOH-terminal carboxyl group are observed as ions having normal isotopic pattern.

    Article Snippet: The unseparated pool of tryptic peptides recovered from the gel matrix was sequenced on a experimental prototype of a hybrid quadrupole Time-Of-Flight tandem mass spectrometer developed by PE Sciex (Ontario, Canada) and University of Manitoba (Winnipeg, Canada) ( ).

    Techniques: Immunoprecipitation, SDS Page, Staining, Migration, Molecular Weight, Sequencing, Mass Spectrometry, Isolation, Purification, Isotopic Labeling, Labeling

    UPLC-ESI-QTOF-MS analysis with selected ion monitoring of epicatechin glucoside in developing M. truncatula seed. A, Extract of seed of mutant line NF0977. B, Extract of seed of wild-type R108. The peak in B corresponds to glucosylated epicatechin (Epi-glc;

    Journal: Plant Physiology

    Article Title: A WD40 Repeat Protein from Medicago truncatula Is Necessary for Tissue-Specific Anthocyanin and Proanthocyanidin Biosynthesis But Not for Trichome Development 1 Is Necessary for Tissue-Specific Anthocyanin and Proanthocyanidin Biosynthesis But Not for Trichome Development 1 [W] Is Necessary for Tissue-Specific Anthocyanin and Proanthocyanidin Biosynthesis But Not for Trichome Development 1 [W

    doi: 10.1104/pp.109.144022

    Figure Lengend Snippet: UPLC-ESI-QTOF-MS analysis with selected ion monitoring of epicatechin glucoside in developing M. truncatula seed. A, Extract of seed of mutant line NF0977. B, Extract of seed of wild-type R108. The peak in B corresponds to glucosylated epicatechin (Epi-glc;

    Article Snippet: Samples were centrifuged at 2,900 g for 30 min, and the supernatants were transferred to liquid chromatography vials and analyzed with a Waters Acquit UPLC system fitted with a hybrid quadrupole time-of-flight (QTOF) Premier mass spectrometer (Waters).

    Techniques: Mass Spectrometry, Mutagenesis, Gas Chromatography

    Nonaqueous ESI-MS analysis of pilin protein. (A) Mass spectrum of the intact protein sample acquired on the Q-TOF2 mass spectrometer. The molecular mass profile derived from this mass spectrum is presented in the inset. (B) Top-down MS/MS spectrum of

    Journal: Journal of Bacteriology

    Article Title: Genetic and Mass Spectrometry Analyses of the Unusual Type IV-Like Pili of the Archaeon Methanococcus maripaludis ▿

    doi: 10.1128/JB.00822-10

    Figure Lengend Snippet: Nonaqueous ESI-MS analysis of pilin protein. (A) Mass spectrum of the intact protein sample acquired on the Q-TOF2 mass spectrometer. The molecular mass profile derived from this mass spectrum is presented in the inset. (B) Top-down MS/MS spectrum of

    Article Snippet: All mass spectra were acquired on a Q-TOF2 hybrid quadrupole time-of-flight mass spectrometer (Waters).

    Techniques: Mass Spectrometry, Derivative Assay

    Hybrid quadrupole orthogonal time-of-flight mass spectrometry (Q-TOF) detects PIB and eight other monoacylphloroglucinols

    Journal: Physiologia plantarum

    Article Title: Identification and biosynthesis of acylphloroglucinols in Hypericum gentianoides

    doi: 10.1111/ppl.12063

    Figure Lengend Snippet: Hybrid quadrupole orthogonal time-of-flight mass spectrometry (Q-TOF) detects PIB and eight other monoacylphloroglucinols

    Article Snippet: High resolution mass spectrometric analysis was performed on a hybrid quadrupole orthogonal time-of-flight mass spectrometer (Waters SYNAPT G2 HDMS, Manchester, U.K.) equipped with an automatic chip-based nanoelectrospray source NanoMate HD (Advion BioSciences, Ithaca, NY).

    Techniques: Mass Spectrometry

    Identification of ions from MALDI TIMS by precursor ion fragmentation and product ion scan . A thin section from the ovarian tumor in Fig. 3 was analyzed using a hybrid quadrupole time-of-flight mass spectrometer (ABI Q-STAR) in negative ionization mode with selection of the shown parent ions for fragmentation and analysis of the product ion spectra. (A and B) Product ion spectrum for each compound ( m/z 778.6 ion was identified as a d18:1/C16:0 ceramide monohexosylsulfatide and m/z 885.6 was most consistent with the shown phosphatidylinositol).

    Journal: Molecular Cancer

    Article Title: Elevation of sulfatides in ovarian cancer: An integrated transcriptomic and lipidomic analysis including tissue-imaging mass spectrometry

    doi: 10.1186/1476-4598-9-186

    Figure Lengend Snippet: Identification of ions from MALDI TIMS by precursor ion fragmentation and product ion scan . A thin section from the ovarian tumor in Fig. 3 was analyzed using a hybrid quadrupole time-of-flight mass spectrometer (ABI Q-STAR) in negative ionization mode with selection of the shown parent ions for fragmentation and analysis of the product ion spectra. (A and B) Product ion spectrum for each compound ( m/z 778.6 ion was identified as a d18:1/C16:0 ceramide monohexosylsulfatide and m/z 885.6 was most consistent with the shown phosphatidylinositol).

    Article Snippet: The major ions of interest (i.e., putative ST) underwent further structural analysis using a hybrid quadrupole time-of-flight mass spectrometer (Q-STAR, Applied Biosystems Foster City, CA) equipped with an O-MALDI source using a 337 nm N2 Laser (30 Hz).

    Techniques: Mass Spectrometry, Selection