flight maldi tof mass spectrometry Thermo Fisher Search Results


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  • 89
    Thermo Fisher flight maldi tof mass spectrometry
    Amino acid sequence alignment of H. volcanii PanA and PanB. Identical residues are shaded in black. Functionally conserved and semiconserved amino acid residues are shaded in grey. Dashes indicate gaps introduced in the protein sequence alignment. Boxed residues were predicted with a > 90% probability to form a coiled-coil conformation (see Materials and Methods). Consensus sequences of the Walker A and B boxes of the P-loop nucleotidase core are indicated below the alignment as GX 2 GXGKT and DEXD, respectively (where X is any amino acid residue). The AAA ATPase second region of homology or SHR motif [(T/S)-(N/S)-X 5 -DXA-X 2 -R-X 2 -RX-(D/E)] is also indicated. The N-terminal sequences of the PanA-His and PanA Δ1-40 -His antigens were identical to residues 2 to 14 and 41 to 51 of the deduced primary sequence, respectively. <t>MALDI-TOF</t> Q-STAR detected the mass spectra of 11 tryptic fragments of the PanB-His antigen, which encompassed 36% of the primary amino acid sequence. The masses (in daltons) and corresponding residue numbers of PanB-His were as follows: 716.3148, 30 to 34; 749.3711, 35 to 40; 1,004.5522, 330 to 337; 1,264.6408, 205 to 261; 1,307.7720, 317 to 328; 1,490.6807, 379 to 392; 1,548.7975, 301 to 313; 1,836.7691, 275 to 289; 2,180.0845, 118 to 137; 2,408.1564, 4 to 24; 2,739.3637, 138 to 162.
    Flight Maldi Tof Mass Spectrometry, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 89/100, based on 189 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher flight mass spectrometry maldi tof mass spectrometer
    Proteome pattern of cervical cancer tissue. Nineteen protein spots on the gel were marked with arrows. Numbered spots were excised from the cancer tissue gel, in-gel digested with trypsin, and identified by <t>MALDI-TOF</t> assay. The results are listed in Table 2 . MALDI-TOF, matrix assisted laser desorption ionization-Time of flight mass spectrometry.
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    86
    Thermo Fisher flight maldi tof mass spectrometry mass spectrometry ms system
    Proteome pattern of cervical cancer tissue. Nineteen protein spots on the gel were marked with arrows. Numbered spots were excised from the cancer tissue gel, in-gel digested with trypsin, and identified by <t>MALDI-TOF</t> assay. The results are listed in Table 2 . MALDI-TOF, matrix assisted laser desorption ionization-Time of flight mass spectrometry.
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    88
    Thermo Fisher matrix assisted laser desorption ionization time of flight maldi tof mass spectrometry
    Proteome pattern of cervical cancer tissue. Nineteen protein spots on the gel were marked with arrows. Numbered spots were excised from the cancer tissue gel, in-gel digested with trypsin, and identified by <t>MALDI-TOF</t> assay. The results are listed in Table 2 . MALDI-TOF, matrix assisted laser desorption ionization-Time of flight mass spectrometry.
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    79
    Thermo Fisher flight maldi tof instrument
    Proteome pattern of cervical cancer tissue. Nineteen protein spots on the gel were marked with arrows. Numbered spots were excised from the cancer tissue gel, in-gel digested with trypsin, and identified by <t>MALDI-TOF</t> assay. The results are listed in Table 2 . MALDI-TOF, matrix assisted laser desorption ionization-Time of flight mass spectrometry.
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    Thermo Fisher flight maldi tof mass spectrometer
    BisC is unable to reduce protein-bound methionyl residues. (A) The primary sequence of MoeB is shown. Peptides whose oxidation status was followed during the experiment are indicated in boxes. (B) <t>MALDI-TOF</t> spectra of peptides generated by trypsin treatment of native MoeB, oxidized MoeB (MoeB ox), and oxidized MoeB repaired with BisC, BisC and MsrB, or MsrA and MsrB.
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    76
    Thermo Fisher flight maldi tof mass spectrograph
    BisC is unable to reduce protein-bound methionyl residues. (A) The primary sequence of MoeB is shown. Peptides whose oxidation status was followed during the experiment are indicated in boxes. (B) <t>MALDI-TOF</t> spectra of peptides generated by trypsin treatment of native MoeB, oxidized MoeB (MoeB ox), and oxidized MoeB repaired with BisC, BisC and MsrB, or MsrA and MsrB.
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    Thermo Fisher maldi tof tof
    BisC is unable to reduce protein-bound methionyl residues. (A) The primary sequence of MoeB is shown. Peptides whose oxidation status was followed during the experiment are indicated in boxes. (B) <t>MALDI-TOF</t> spectra of peptides generated by trypsin treatment of native MoeB, oxidized MoeB (MoeB ox), and oxidized MoeB repaired with BisC, BisC and MsrB, or MsrA and MsrB.
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    Thermo Fisher maldi time of flight
    BisC is unable to reduce protein-bound methionyl residues. (A) The primary sequence of MoeB is shown. Peptides whose oxidation status was followed during the experiment are indicated in boxes. (B) <t>MALDI-TOF</t> spectra of peptides generated by trypsin treatment of native MoeB, oxidized MoeB (MoeB ox), and oxidized MoeB repaired with BisC, BisC and MsrB, or MsrA and MsrB.
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    Thermo Fisher 4800 maldi tof tof
    BisC is unable to reduce protein-bound methionyl residues. (A) The primary sequence of MoeB is shown. Peptides whose oxidation status was followed during the experiment are indicated in boxes. (B) <t>MALDI-TOF</t> spectra of peptides generated by trypsin treatment of native MoeB, oxidized MoeB (MoeB ox), and oxidized MoeB repaired with BisC, BisC and MsrB, or MsrA and MsrB.
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    79
    Thermo Fisher 4800 maldi time of flight
    BisC is unable to reduce protein-bound methionyl residues. (A) The primary sequence of MoeB is shown. Peptides whose oxidation status was followed during the experiment are indicated in boxes. (B) <t>MALDI-TOF</t> spectra of peptides generated by trypsin treatment of native MoeB, oxidized MoeB (MoeB ox), and oxidized MoeB repaired with BisC, BisC and MsrB, or MsrA and MsrB.
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    Thermo Fisher flight maldi tof mass spectrometer vision 2000
    BisC is unable to reduce protein-bound methionyl residues. (A) The primary sequence of MoeB is shown. Peptides whose oxidation status was followed during the experiment are indicated in boxes. (B) <t>MALDI-TOF</t> spectra of peptides generated by trypsin treatment of native MoeB, oxidized MoeB (MoeB ox), and oxidized MoeB repaired with BisC, BisC and MsrB, or MsrA and MsrB.
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    Thermo Fisher flight maldi tof target plate
    BisC is unable to reduce protein-bound methionyl residues. (A) The primary sequence of MoeB is shown. Peptides whose oxidation status was followed during the experiment are indicated in boxes. (B) <t>MALDI-TOF</t> spectra of peptides generated by trypsin treatment of native MoeB, oxidized MoeB (MoeB ox), and oxidized MoeB repaired with BisC, BisC and MsrB, or MsrA and MsrB.
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    Thermo Fisher abi 4700 maldi tof tof
    BisC is unable to reduce protein-bound methionyl residues. (A) The primary sequence of MoeB is shown. Peptides whose oxidation status was followed during the experiment are indicated in boxes. (B) <t>MALDI-TOF</t> spectra of peptides generated by trypsin treatment of native MoeB, oxidized MoeB (MoeB ox), and oxidized MoeB repaired with BisC, BisC and MsrB, or MsrA and MsrB.
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    94
    Thermo Fisher matrix assisted laser desorption ionization time of flight mass spectrometry
    BisC is unable to reduce protein-bound methionyl residues. (A) The primary sequence of MoeB is shown. Peptides whose oxidation status was followed during the experiment are indicated in boxes. (B) <t>MALDI-TOF</t> spectra of peptides generated by trypsin treatment of native MoeB, oxidized MoeB (MoeB ox), and oxidized MoeB repaired with BisC, BisC and MsrB, or MsrA and MsrB.
    Matrix Assisted Laser Desorption Ionization Time Of Flight Mass Spectrometry, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 398 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    Thermo Fisher maldi time of flight mass spectrometer
    <t>MALDI-TOF-ESI</t> mass spectrometry data and amino acid sequence alignment of KD1 L17R -K T with the starting molecule (KD1 L17R -V T ) and BPTI. (A) Mass spectrometry data of KD1 L17R -K T obtained using an Applied Biosystems Voyager <t>DE-STR.</t> The spectra were calibrated; thus, the masses should be within 0.1% of the theoretical values. (B) Amino acid sequences of KD1 L17R -V T and the two KD1 L17R -K T species: one with N-terminus sequence Gly-Asn-Asn-Ala-Glu-Ile (∼80%) and a second with N-terminus sequence Asn-Ala-Glu-Ile (∼20%). Note that the minor sequence is internal to the major sequence starting at cycle 3 asparagine and that the calculated difference in MW between the two species is 171 Da; this is consistent with the mass spectrometry data shown in panel A. We infer that IIa or a contaminating protease cleaved the peptide bonds (shown by ↓) between amino acids Thr–Gly and Asn–Asn on the N-terminal side and between Lys–Val on the C-terminal side of KD1 L17R -V T . The numbering system used is that of BPTI (prototype Kunitz inhibitor). The N-terminal Gly-Ser-His-Met sequence in KD1 L17R -V T is derived from the IIa cleavage site introduced during cloning. The P1 and P2′ subsites recognized by plasmin are marked.
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    81
    Thermo Fisher matrix assisted laser desorption ionization tandem time of flight mass spectrometry
    <t>MALDI-TOF-ESI</t> mass spectrometry data and amino acid sequence alignment of KD1 L17R -K T with the starting molecule (KD1 L17R -V T ) and BPTI. (A) Mass spectrometry data of KD1 L17R -K T obtained using an Applied Biosystems Voyager <t>DE-STR.</t> The spectra were calibrated; thus, the masses should be within 0.1% of the theoretical values. (B) Amino acid sequences of KD1 L17R -V T and the two KD1 L17R -K T species: one with N-terminus sequence Gly-Asn-Asn-Ala-Glu-Ile (∼80%) and a second with N-terminus sequence Asn-Ala-Glu-Ile (∼20%). Note that the minor sequence is internal to the major sequence starting at cycle 3 asparagine and that the calculated difference in MW between the two species is 171 Da; this is consistent with the mass spectrometry data shown in panel A. We infer that IIa or a contaminating protease cleaved the peptide bonds (shown by ↓) between amino acids Thr–Gly and Asn–Asn on the N-terminal side and between Lys–Val on the C-terminal side of KD1 L17R -V T . The numbering system used is that of BPTI (prototype Kunitz inhibitor). The N-terminal Gly-Ser-His-Met sequence in KD1 L17R -V T is derived from the IIa cleavage site introduced during cloning. The P1 and P2′ subsites recognized by plasmin are marked.
    Matrix Assisted Laser Desorption Ionization Tandem Time Of Flight Mass Spectrometry, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 81/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    77
    Thermo Fisher maldi tandem time of flight tof tof 4700 proteomics analyzer
    <t>MALDI-TOF-ESI</t> mass spectrometry data and amino acid sequence alignment of KD1 L17R -K T with the starting molecule (KD1 L17R -V T ) and BPTI. (A) Mass spectrometry data of KD1 L17R -K T obtained using an Applied Biosystems Voyager <t>DE-STR.</t> The spectra were calibrated; thus, the masses should be within 0.1% of the theoretical values. (B) Amino acid sequences of KD1 L17R -V T and the two KD1 L17R -K T species: one with N-terminus sequence Gly-Asn-Asn-Ala-Glu-Ile (∼80%) and a second with N-terminus sequence Asn-Ala-Glu-Ile (∼20%). Note that the minor sequence is internal to the major sequence starting at cycle 3 asparagine and that the calculated difference in MW between the two species is 171 Da; this is consistent with the mass spectrometry data shown in panel A. We infer that IIa or a contaminating protease cleaved the peptide bonds (shown by ↓) between amino acids Thr–Gly and Asn–Asn on the N-terminal side and between Lys–Val on the C-terminal side of KD1 L17R -V T . The numbering system used is that of BPTI (prototype Kunitz inhibitor). The N-terminal Gly-Ser-His-Met sequence in KD1 L17R -V T is derived from the IIa cleavage site introduced during cloning. The P1 and P2′ subsites recognized by plasmin are marked.
    Maldi Tandem Time Of Flight Tof Tof 4700 Proteomics Analyzer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 77/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    77
    Thermo Fisher flight maldi tof tof 4800 mass spectrometer
    <t>MALDI-TOF-ESI</t> mass spectrometry data and amino acid sequence alignment of KD1 L17R -K T with the starting molecule (KD1 L17R -V T ) and BPTI. (A) Mass spectrometry data of KD1 L17R -K T obtained using an Applied Biosystems Voyager <t>DE-STR.</t> The spectra were calibrated; thus, the masses should be within 0.1% of the theoretical values. (B) Amino acid sequences of KD1 L17R -V T and the two KD1 L17R -K T species: one with N-terminus sequence Gly-Asn-Asn-Ala-Glu-Ile (∼80%) and a second with N-terminus sequence Asn-Ala-Glu-Ile (∼20%). Note that the minor sequence is internal to the major sequence starting at cycle 3 asparagine and that the calculated difference in MW between the two species is 171 Da; this is consistent with the mass spectrometry data shown in panel A. We infer that IIa or a contaminating protease cleaved the peptide bonds (shown by ↓) between amino acids Thr–Gly and Asn–Asn on the N-terminal side and between Lys–Val on the C-terminal side of KD1 L17R -V T . The numbering system used is that of BPTI (prototype Kunitz inhibitor). The N-terminal Gly-Ser-His-Met sequence in KD1 L17R -V T is derived from the IIa cleavage site introduced during cloning. The P1 and P2′ subsites recognized by plasmin are marked.
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    Thermo Fisher 4800 maldi tandem time of flight analyzer
    <t>MALDI-TOF-ESI</t> mass spectrometry data and amino acid sequence alignment of KD1 L17R -K T with the starting molecule (KD1 L17R -V T ) and BPTI. (A) Mass spectrometry data of KD1 L17R -K T obtained using an Applied Biosystems Voyager <t>DE-STR.</t> The spectra were calibrated; thus, the masses should be within 0.1% of the theoretical values. (B) Amino acid sequences of KD1 L17R -V T and the two KD1 L17R -K T species: one with N-terminus sequence Gly-Asn-Asn-Ala-Glu-Ile (∼80%) and a second with N-terminus sequence Asn-Ala-Glu-Ile (∼20%). Note that the minor sequence is internal to the major sequence starting at cycle 3 asparagine and that the calculated difference in MW between the two species is 171 Da; this is consistent with the mass spectrometry data shown in panel A. We infer that IIa or a contaminating protease cleaved the peptide bonds (shown by ↓) between amino acids Thr–Gly and Asn–Asn on the N-terminal side and between Lys–Val on the C-terminal side of KD1 L17R -V T . The numbering system used is that of BPTI (prototype Kunitz inhibitor). The N-terminal Gly-Ser-His-Met sequence in KD1 L17R -V T is derived from the IIa cleavage site introduced during cloning. The P1 and P2′ subsites recognized by plasmin are marked.
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    Thermo Fisher 4700 proteomic analyzer maldi time of flight maldi tof mass spectrometer
    <t>MALDI-TOF-ESI</t> mass spectrometry data and amino acid sequence alignment of KD1 L17R -K T with the starting molecule (KD1 L17R -V T ) and BPTI. (A) Mass spectrometry data of KD1 L17R -K T obtained using an Applied Biosystems Voyager <t>DE-STR.</t> The spectra were calibrated; thus, the masses should be within 0.1% of the theoretical values. (B) Amino acid sequences of KD1 L17R -V T and the two KD1 L17R -K T species: one with N-terminus sequence Gly-Asn-Asn-Ala-Glu-Ile (∼80%) and a second with N-terminus sequence Asn-Ala-Glu-Ile (∼20%). Note that the minor sequence is internal to the major sequence starting at cycle 3 asparagine and that the calculated difference in MW between the two species is 171 Da; this is consistent with the mass spectrometry data shown in panel A. We infer that IIa or a contaminating protease cleaved the peptide bonds (shown by ↓) between amino acids Thr–Gly and Asn–Asn on the N-terminal side and between Lys–Val on the C-terminal side of KD1 L17R -V T . The numbering system used is that of BPTI (prototype Kunitz inhibitor). The N-terminal Gly-Ser-His-Met sequence in KD1 L17R -V T is derived from the IIa cleavage site introduced during cloning. The P1 and P2′ subsites recognized by plasmin are marked.
    4700 Proteomic Analyzer Maldi Time Of Flight Maldi Tof Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 77/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher matrix assisted laser desorption ionization maldi time of flight plates
    <t>MALDI-TOF-ESI</t> mass spectrometry data and amino acid sequence alignment of KD1 L17R -K T with the starting molecule (KD1 L17R -V T ) and BPTI. (A) Mass spectrometry data of KD1 L17R -K T obtained using an Applied Biosystems Voyager <t>DE-STR.</t> The spectra were calibrated; thus, the masses should be within 0.1% of the theoretical values. (B) Amino acid sequences of KD1 L17R -V T and the two KD1 L17R -K T species: one with N-terminus sequence Gly-Asn-Asn-Ala-Glu-Ile (∼80%) and a second with N-terminus sequence Asn-Ala-Glu-Ile (∼20%). Note that the minor sequence is internal to the major sequence starting at cycle 3 asparagine and that the calculated difference in MW between the two species is 171 Da; this is consistent with the mass spectrometry data shown in panel A. We infer that IIa or a contaminating protease cleaved the peptide bonds (shown by ↓) between amino acids Thr–Gly and Asn–Asn on the N-terminal side and between Lys–Val on the C-terminal side of KD1 L17R -V T . The numbering system used is that of BPTI (prototype Kunitz inhibitor). The N-terminal Gly-Ser-His-Met sequence in KD1 L17R -V T is derived from the IIa cleavage site introduced during cloning. The P1 and P2′ subsites recognized by plasmin are marked.
    Matrix Assisted Laser Desorption Ionization Maldi Time Of Flight Plates, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 77/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Amino acid sequence alignment of H. volcanii PanA and PanB. Identical residues are shaded in black. Functionally conserved and semiconserved amino acid residues are shaded in grey. Dashes indicate gaps introduced in the protein sequence alignment. Boxed residues were predicted with a > 90% probability to form a coiled-coil conformation (see Materials and Methods). Consensus sequences of the Walker A and B boxes of the P-loop nucleotidase core are indicated below the alignment as GX 2 GXGKT and DEXD, respectively (where X is any amino acid residue). The AAA ATPase second region of homology or SHR motif [(T/S)-(N/S)-X 5 -DXA-X 2 -R-X 2 -RX-(D/E)] is also indicated. The N-terminal sequences of the PanA-His and PanA Δ1-40 -His antigens were identical to residues 2 to 14 and 41 to 51 of the deduced primary sequence, respectively. MALDI-TOF Q-STAR detected the mass spectra of 11 tryptic fragments of the PanB-His antigen, which encompassed 36% of the primary amino acid sequence. The masses (in daltons) and corresponding residue numbers of PanB-His were as follows: 716.3148, 30 to 34; 749.3711, 35 to 40; 1,004.5522, 330 to 337; 1,264.6408, 205 to 261; 1,307.7720, 317 to 328; 1,490.6807, 379 to 392; 1,548.7975, 301 to 313; 1,836.7691, 275 to 289; 2,180.0845, 118 to 137; 2,408.1564, 4 to 24; 2,739.3637, 138 to 162.

    Journal: Journal of Bacteriology

    Article Title: Differential Regulation of the PanA and PanB Proteasome-Activating Nucleotidase and 20S Proteasomal Proteins of the Haloarchaeon Haloferax volcanii †

    doi: 10.1128/JB.186.22.7763-7772.2004

    Figure Lengend Snippet: Amino acid sequence alignment of H. volcanii PanA and PanB. Identical residues are shaded in black. Functionally conserved and semiconserved amino acid residues are shaded in grey. Dashes indicate gaps introduced in the protein sequence alignment. Boxed residues were predicted with a > 90% probability to form a coiled-coil conformation (see Materials and Methods). Consensus sequences of the Walker A and B boxes of the P-loop nucleotidase core are indicated below the alignment as GX 2 GXGKT and DEXD, respectively (where X is any amino acid residue). The AAA ATPase second region of homology or SHR motif [(T/S)-(N/S)-X 5 -DXA-X 2 -R-X 2 -RX-(D/E)] is also indicated. The N-terminal sequences of the PanA-His and PanA Δ1-40 -His antigens were identical to residues 2 to 14 and 41 to 51 of the deduced primary sequence, respectively. MALDI-TOF Q-STAR detected the mass spectra of 11 tryptic fragments of the PanB-His antigen, which encompassed 36% of the primary amino acid sequence. The masses (in daltons) and corresponding residue numbers of PanB-His were as follows: 716.3148, 30 to 34; 749.3711, 35 to 40; 1,004.5522, 330 to 337; 1,264.6408, 205 to 261; 1,307.7720, 317 to 328; 1,490.6807, 379 to 392; 1,548.7975, 301 to 313; 1,836.7691, 275 to 289; 2,180.0845, 118 to 137; 2,408.1564, 4 to 24; 2,739.3637, 138 to 162.

    Article Snippet: Prior to antibody preparation, the N-terminal sequences of PanAΔ1-40 -His and PanA-His were determined by Edman degradation, and the mass spectra of the tryptic fragments of PanB-His were determined by matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometry (Applied Biosystems QSTAR XL hybrid LC/MS/MS; University of Florida ICBR Protein Chemistry Core).

    Techniques: Sequencing

    Purification and MALDI-TOF mass analysis of MIFs. A , MALDI-TOF mass spectrum of purified huMIF. The inset shows silver-stained huMIF purified sequentially through Ni-NTA and then a Sephadex 75 column and electrophoresed in a 4–20% gradient gel.

    Journal: The Journal of Biological Chemistry

    Article Title: Novel Anti-inflammatory Activity of Epoxyazadiradione against Macrophage Migration Inhibitory Factor

    doi: 10.1074/jbc.M112.341321

    Figure Lengend Snippet: Purification and MALDI-TOF mass analysis of MIFs. A , MALDI-TOF mass spectrum of purified huMIF. The inset shows silver-stained huMIF purified sequentially through Ni-NTA and then a Sephadex 75 column and electrophoresed in a 4–20% gradient gel.

    Article Snippet: The molecular weights of the purified huMIF, Pf MIF, and Py MIF were confirmed by matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectroscopy (Applied Biosystems, Foster City, CA), which showed exact molecular masses ( m / z ) of 13.430, 13.266, and 13.251 kDa, respectively ( , A , B , and C ).

    Techniques: Purification, Staining

    Proteome pattern of cervical cancer tissue. Nineteen protein spots on the gel were marked with arrows. Numbered spots were excised from the cancer tissue gel, in-gel digested with trypsin, and identified by MALDI-TOF assay. The results are listed in Table 2 . MALDI-TOF, matrix assisted laser desorption ionization-Time of flight mass spectrometry.

    Journal: Yonsei Medical Journal

    Article Title: Expression of Heat Shock Protein 60 kDa Is Upregulated in Cervical Cancer

    doi: 10.3349/ymj.2009.50.3.399

    Figure Lengend Snippet: Proteome pattern of cervical cancer tissue. Nineteen protein spots on the gel were marked with arrows. Numbered spots were excised from the cancer tissue gel, in-gel digested with trypsin, and identified by MALDI-TOF assay. The results are listed in Table 2 . MALDI-TOF, matrix assisted laser desorption ionization-Time of flight mass spectrometry.

    Article Snippet: Peptides masses were analyzed using Voyager DE Matrix assisted laser desorption ionization-Time of flight mass spectrometry (MALDI-TOF) mass spectrometer (Applied Biosystems, Foster City, USA).

    Techniques: Mass Spectrometry

    Proteome pattern of normal cervical tissue. Eleven protein spots on the gel were marked with arrows. Numbered spots were excised from the normal tissue gel, in-gel digested with trypsin, and identified by MALDI-TOF assay. The results are listed in Table 1 . MALDI-TOF, matrix assisted laser desorption ionization-Time of flight mass spectrometry.

    Journal: Yonsei Medical Journal

    Article Title: Expression of Heat Shock Protein 60 kDa Is Upregulated in Cervical Cancer

    doi: 10.3349/ymj.2009.50.3.399

    Figure Lengend Snippet: Proteome pattern of normal cervical tissue. Eleven protein spots on the gel were marked with arrows. Numbered spots were excised from the normal tissue gel, in-gel digested with trypsin, and identified by MALDI-TOF assay. The results are listed in Table 1 . MALDI-TOF, matrix assisted laser desorption ionization-Time of flight mass spectrometry.

    Article Snippet: Peptides masses were analyzed using Voyager DE Matrix assisted laser desorption ionization-Time of flight mass spectrometry (MALDI-TOF) mass spectrometer (Applied Biosystems, Foster City, USA).

    Techniques: Mass Spectrometry

    BisC is unable to reduce protein-bound methionyl residues. (A) The primary sequence of MoeB is shown. Peptides whose oxidation status was followed during the experiment are indicated in boxes. (B) MALDI-TOF spectra of peptides generated by trypsin treatment of native MoeB, oxidized MoeB (MoeB ox), and oxidized MoeB repaired with BisC, BisC and MsrB, or MsrA and MsrB.

    Journal: Journal of Bacteriology

    Article Title: Methionine Sulfoxide Reduction and Assimilation in Escherichia coli: New Role for the Biotin Sulfoxide Reductase BisC

    doi: 10.1128/JB.187.1.231-237.2005

    Figure Lengend Snippet: BisC is unable to reduce protein-bound methionyl residues. (A) The primary sequence of MoeB is shown. Peptides whose oxidation status was followed during the experiment are indicated in boxes. (B) MALDI-TOF spectra of peptides generated by trypsin treatment of native MoeB, oxidized MoeB (MoeB ox), and oxidized MoeB repaired with BisC, BisC and MsrB, or MsrA and MsrB.

    Article Snippet: Isotope 12 C masses were determined in the positive ion reflector mode with a matrix-assisted laser desorption ionization-time of flight (MALDI-TOF)-mass spectrometer Voyager DE-RP (Applied Biosystems) and internal calibration.

    Techniques: Sequencing, Generated

    MALDI-TOF-ESI mass spectrometry data and amino acid sequence alignment of KD1 L17R -K T with the starting molecule (KD1 L17R -V T ) and BPTI. (A) Mass spectrometry data of KD1 L17R -K T obtained using an Applied Biosystems Voyager DE-STR. The spectra were calibrated; thus, the masses should be within 0.1% of the theoretical values. (B) Amino acid sequences of KD1 L17R -V T and the two KD1 L17R -K T species: one with N-terminus sequence Gly-Asn-Asn-Ala-Glu-Ile (∼80%) and a second with N-terminus sequence Asn-Ala-Glu-Ile (∼20%). Note that the minor sequence is internal to the major sequence starting at cycle 3 asparagine and that the calculated difference in MW between the two species is 171 Da; this is consistent with the mass spectrometry data shown in panel A. We infer that IIa or a contaminating protease cleaved the peptide bonds (shown by ↓) between amino acids Thr–Gly and Asn–Asn on the N-terminal side and between Lys–Val on the C-terminal side of KD1 L17R -V T . The numbering system used is that of BPTI (prototype Kunitz inhibitor). The N-terminal Gly-Ser-His-Met sequence in KD1 L17R -V T is derived from the IIa cleavage site introduced during cloning. The P1 and P2′ subsites recognized by plasmin are marked.

    Journal: Biochemistry

    Article Title: Decoy Plasminogen Receptor Containing a Selective Kunitz-Inhibitory Domain

    doi: 10.1021/bi401584b

    Figure Lengend Snippet: MALDI-TOF-ESI mass spectrometry data and amino acid sequence alignment of KD1 L17R -K T with the starting molecule (KD1 L17R -V T ) and BPTI. (A) Mass spectrometry data of KD1 L17R -K T obtained using an Applied Biosystems Voyager DE-STR. The spectra were calibrated; thus, the masses should be within 0.1% of the theoretical values. (B) Amino acid sequences of KD1 L17R -V T and the two KD1 L17R -K T species: one with N-terminus sequence Gly-Asn-Asn-Ala-Glu-Ile (∼80%) and a second with N-terminus sequence Asn-Ala-Glu-Ile (∼20%). Note that the minor sequence is internal to the major sequence starting at cycle 3 asparagine and that the calculated difference in MW between the two species is 171 Da; this is consistent with the mass spectrometry data shown in panel A. We infer that IIa or a contaminating protease cleaved the peptide bonds (shown by ↓) between amino acids Thr–Gly and Asn–Asn on the N-terminal side and between Lys–Val on the C-terminal side of KD1 L17R -V T . The numbering system used is that of BPTI (prototype Kunitz inhibitor). The N-terminal Gly-Ser-His-Met sequence in KD1 L17R -V T is derived from the IIa cleavage site introduced during cloning. The P1 and P2′ subsites recognized by plasmin are marked.

    Article Snippet: A Voyager DE-STR MALDI time-of-flight mass spectrometer (Applied Biosystems, Foster City, CA) operating in the linear mode was used for the MALDI-MS measurements.

    Techniques: Mass Spectrometry, Sequencing, Derivative Assay, Clone Assay

    Identification of two randomly selected differential expression proteins (DEP) by using MALDI-TOF-MS (MS/MS) spectrum for parts of the peptides of these proteins.

    Journal: Scientific Reports

    Article Title: A plasma proteomics method reveals links between ischemic stroke and MTHFR C677T genotype

    doi: 10.1038/s41598-017-13542-6

    Figure Lengend Snippet: Identification of two randomly selected differential expression proteins (DEP) by using MALDI-TOF-MS (MS/MS) spectrum for parts of the peptides of these proteins.

    Article Snippet: MALDI-TOF-MS analysis: identification of the differential protein points Seven protein spots with significant differences were selected in the gel for an API 4800 cascade time-of-flight mass spectrometer MALDI-TOF/TOF (Applied Biosystems) analysis.

    Techniques: Expressing, Mass Spectrometry

    MALDI-TOF MS peptide maps of HNRNPH1 Protein spot of interest was excised from the gels and de-stained, washed, dehydrated, and enzymolyzed. Peptides were extracted and freeze-dried. The peptide mixture was analyzed with MALDI-TOF MS

    Journal: Journal of Zhejiang University. Science. B

    Article Title: Proteomic analysis of human umbilical vein endothelial cells exposed to PM2.5 *

    doi: 10.1631/jzus.B1700103

    Figure Lengend Snippet: MALDI-TOF MS peptide maps of HNRNPH1 Protein spot of interest was excised from the gels and de-stained, washed, dehydrated, and enzymolyzed. Peptides were extracted and freeze-dried. The peptide mixture was analyzed with MALDI-TOF MS

    Article Snippet: Protein with average increase or decrease more than 1.5-fold compared with the control group was designated as differentially expressed protein and identified with a matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometer (Applied Biosystem, USA).

    Techniques: Mass Spectrometry, Staining