flight maldi tof mass spectrometry  (Thermo Fisher)


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    Structured Review

    Thermo Fisher flight maldi tof mass spectrometry
    GPC and mass spectra of four-arm poly(NIPAAm) ( 2 ). GPC trace of the 4-armed poly(NIPAAm) (left); <t>MALDI-TOF</t> spectra before (middle) and after (right) aminolysis.
    Flight Maldi Tof Mass Spectrometry, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 61 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Synthesis of Maleimide-End Functionalized Star Polymers and Multimeric Protein-Polymer Conjugates"

    Article Title: Synthesis of Maleimide-End Functionalized Star Polymers and Multimeric Protein-Polymer Conjugates

    Journal: Macromolecules

    doi: 10.1021/ma901540p

    GPC and mass spectra of four-arm poly(NIPAAm) ( 2 ). GPC trace of the 4-armed poly(NIPAAm) (left); MALDI-TOF spectra before (middle) and after (right) aminolysis.
    Figure Legend Snippet: GPC and mass spectra of four-arm poly(NIPAAm) ( 2 ). GPC trace of the 4-armed poly(NIPAAm) (left); MALDI-TOF spectra before (middle) and after (right) aminolysis.

    Techniques Used: Gel Permeation Chromatography

    2) Product Images from "Isolation and Biochemical Characterization of Apios Tuber Lectin"

    Article Title: Isolation and Biochemical Characterization of Apios Tuber Lectin

    Journal: Molecules

    doi: 10.3390/molecules20010987

    Molecular mass determination of Apios tuber lectin. ( A ) Size exclusion chromatography on a PC200S (N) column (5 μm, 7.8 × 300 nm) in 50 mM HEPES (pH 6.9) containing 0.25 M NaCl and 5 mM CaCl 2 as the mobile phase. Flow rate: 0.8 mL/min; UV detection: 280 nm. ( B ) MALDI-TOF mass spectral analysis.
    Figure Legend Snippet: Molecular mass determination of Apios tuber lectin. ( A ) Size exclusion chromatography on a PC200S (N) column (5 μm, 7.8 × 300 nm) in 50 mM HEPES (pH 6.9) containing 0.25 M NaCl and 5 mM CaCl 2 as the mobile phase. Flow rate: 0.8 mL/min; UV detection: 280 nm. ( B ) MALDI-TOF mass spectral analysis.

    Techniques Used: Size-exclusion Chromatography, Flow Cytometry

    3) Product Images from "An Engineered Saccharomyces cerevisiae Strain Binds the Broadly Neutralizing Human Immunodeficiency Virus Type 1 Antibody 2G12 and Elicits Mannose-Specific gp120-Binding Antibodies "

    Article Title: An Engineered Saccharomyces cerevisiae Strain Binds the Broadly Neutralizing Human Immunodeficiency Virus Type 1 Antibody 2G12 and Elicits Mannose-Specific gp120-Binding Antibodies

    Journal: Journal of Virology

    doi: 10.1128/JVI.00412-08

    Cross-reactivity of 2G12 with TM yeast expressing mostly Man8 glycans. (A) MALDI-TOF MS was performed on permethylated glycans, released from homogenized TM yeast with PNGase F. The major mass peak at a mass-to-charge ratio ( m/z ) of 2191.73 is representative
    Figure Legend Snippet: Cross-reactivity of 2G12 with TM yeast expressing mostly Man8 glycans. (A) MALDI-TOF MS was performed on permethylated glycans, released from homogenized TM yeast with PNGase F. The major mass peak at a mass-to-charge ratio ( m/z ) of 2191.73 is representative

    Techniques Used: Expressing, Mass Spectrometry

    4) Product Images from "Binding Partners for the UL11 Tegument Protein of Herpes Simplex Virus Type 1"

    Article Title: Binding Partners for the UL11 Tegument Protein of Herpes Simplex Virus Type 1

    Journal: Journal of Virology

    doi: 10.1128/JVI.77.21.11417-11424.2003

    Direct analysis of the 40-kDa protein by MS. (A) Visualization of the 40-kDa band by zinc staining. The 40-kDa protein (denoted by an arrowhead) was pulled out of unlabeled, HSV-1-infected cell lysates with GST.UL11 H .d51-96 and separated by SDS-PAGE. The gel was negatively stained with a Bio-Rad zinc stain kit; the isolated 40-kDa band was cut from the gel, digested with trypsin, and analyzed by MALDI-TOF MS. Asterisks denote the positions of the GST derivatives on the gel. Plus or minus signs indicate that GST proteins were mixed with HSV-1-infected cell lysates or not, respectively, prior to being loaded on the gel. Numbers at left indicate kilodaltons. (B) MS-MS spectrum of the 1,646-Da tryptic peptide. The 10 most abundant peptide fragments on the MS spectrum were identified and further analyzed by tandem MS-MS ion fragment analysis. The resulting MS-MS spectrum of the 1,646-Da peptide was used to determine its sequence (inset), which was then examined for matches with the sequences of all known proteins. Residue numbers within the HSV-1 UL16 protein are indicated below the inset. Asterisks denote MS-MS peaks that were used in elucidating the 1,646-Da peptide sequence.
    Figure Legend Snippet: Direct analysis of the 40-kDa protein by MS. (A) Visualization of the 40-kDa band by zinc staining. The 40-kDa protein (denoted by an arrowhead) was pulled out of unlabeled, HSV-1-infected cell lysates with GST.UL11 H .d51-96 and separated by SDS-PAGE. The gel was negatively stained with a Bio-Rad zinc stain kit; the isolated 40-kDa band was cut from the gel, digested with trypsin, and analyzed by MALDI-TOF MS. Asterisks denote the positions of the GST derivatives on the gel. Plus or minus signs indicate that GST proteins were mixed with HSV-1-infected cell lysates or not, respectively, prior to being loaded on the gel. Numbers at left indicate kilodaltons. (B) MS-MS spectrum of the 1,646-Da tryptic peptide. The 10 most abundant peptide fragments on the MS spectrum were identified and further analyzed by tandem MS-MS ion fragment analysis. The resulting MS-MS spectrum of the 1,646-Da peptide was used to determine its sequence (inset), which was then examined for matches with the sequences of all known proteins. Residue numbers within the HSV-1 UL16 protein are indicated below the inset. Asterisks denote MS-MS peaks that were used in elucidating the 1,646-Da peptide sequence.

    Techniques Used: Mass Spectrometry, Staining, Infection, SDS Page, Isolation, Sequencing

    5) Product Images from "Characterization of Amylolysin, a Novel Lantibiotic from Bacillus amyloliquefaciens GA1"

    Article Title: Characterization of Amylolysin, a Novel Lantibiotic from Bacillus amyloliquefaciens GA1

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0083037

    MALDI-TOF MS and LC-MS analysis of amylolysin. Mass spectrum of purified amylolysin sample was recorded in negative mode. Insert: LC-MS chromatograms of commercial lanthionine standard and amylolysin hydrolysate. Intensity (%, Y-scale) was recorded by setting the SQD mass analyzer on the specific mass of lanthionine (315 Da).
    Figure Legend Snippet: MALDI-TOF MS and LC-MS analysis of amylolysin. Mass spectrum of purified amylolysin sample was recorded in negative mode. Insert: LC-MS chromatograms of commercial lanthionine standard and amylolysin hydrolysate. Intensity (%, Y-scale) was recorded by setting the SQD mass analyzer on the specific mass of lanthionine (315 Da).

    Techniques Used: Mass Spectrometry, Liquid Chromatography with Mass Spectroscopy, Purification

    6) Product Images from "Structure, Antimicrobial Activities and Mode of Interaction with Membranes of Bovel Phylloseptins from the Painted-Belly Leaf Frog, Phyllomedusa sauvagii"

    Article Title: Structure, Antimicrobial Activities and Mode of Interaction with Membranes of Bovel Phylloseptins from the Painted-Belly Leaf Frog, Phyllomedusa sauvagii

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0070782

    Reversed-phase HPLC chromatogram of P. sauvagii skin extract prepurified on a sep-pak C18 cartridge (A, full scale; B, zoom). The sample was injected on a semi-preparative Nucleosil C18 column eluted at 4 mL/min with a 0–70% linear gradient of acetonitrile in 0.1% TFA/water (1% ACN/min). Fractions of 4 mL were collected, lyophilized, and analyzed. The position of the mature PLSs is indicated by an arrow (PLS-S3 and PLS-S6 were not detected). The identification of PLSs was achieved by MALDI-TOF-MS and MS/MS (Supporting information, Fig. S1 A–C and S2 A–C ).
    Figure Legend Snippet: Reversed-phase HPLC chromatogram of P. sauvagii skin extract prepurified on a sep-pak C18 cartridge (A, full scale; B, zoom). The sample was injected on a semi-preparative Nucleosil C18 column eluted at 4 mL/min with a 0–70% linear gradient of acetonitrile in 0.1% TFA/water (1% ACN/min). Fractions of 4 mL were collected, lyophilized, and analyzed. The position of the mature PLSs is indicated by an arrow (PLS-S3 and PLS-S6 were not detected). The identification of PLSs was achieved by MALDI-TOF-MS and MS/MS (Supporting information, Fig. S1 A–C and S2 A–C ).

    Techniques Used: High Performance Liquid Chromatography, Injection, Mass Spectrometry

    7) Product Images from "Cationized liposomal keto-mycolic acids isolated from Mycobacterium bovis bacillus Calmette-Guérin induce antitumor immunity in a syngeneic murine bladder cancer model"

    Article Title: Cationized liposomal keto-mycolic acids isolated from Mycobacterium bovis bacillus Calmette-Guérin induce antitumor immunity in a syngeneic murine bladder cancer model

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0209196

    a: Thin layer chromatography of mycolic acid (MA) subclasses. The TLC plate was developed with n-hexane-diethyl ether (80:20, v/v; four runs) and visualized by spraying with phosphomolybdic acid. b–d: MALDI-TOF mass spectra of MA from M . bovis BCG Tokyo 172, α-MA (b), methoxy-MA (c), and keto-MA (d) . e: The chemical structure of MA subclass derived from M . bovis BCG Tokyo 172 .
    Figure Legend Snippet: a: Thin layer chromatography of mycolic acid (MA) subclasses. The TLC plate was developed with n-hexane-diethyl ether (80:20, v/v; four runs) and visualized by spraying with phosphomolybdic acid. b–d: MALDI-TOF mass spectra of MA from M . bovis BCG Tokyo 172, α-MA (b), methoxy-MA (c), and keto-MA (d) . e: The chemical structure of MA subclass derived from M . bovis BCG Tokyo 172 .

    Techniques Used: Thin Layer Chromatography, Derivative Assay

    8) Product Images from "Physical and Functional Interaction between DNA Ligase III? and Poly(ADP-Ribose) Polymerase 1 in DNA Single-Strand Break Repair"

    Article Title: Physical and Functional Interaction between DNA Ligase III? and Poly(ADP-Ribose) Polymerase 1 in DNA Single-Strand Break Repair

    Journal: Molecular and Cellular Biology

    doi: 10.1128/MCB.23.16.5919-5927.2003

    Identification of DNA ligase III-associated proteins by affinity chromatography. A HeLa nuclear extract was fractionated by using a DNA ligase III affinity chromatography column as described in Materials and Methods. (A) Proteins in comparable fractions eluted with 0.3 M NaCl from the beads liganded by GST and by GST-DNA ligase III (Lig III) were detected by silver staining after separation by SDS-PAGE. The polypeptides indicated were identified by MALDI-TOF mass spectrometry. The identities of PARP-1, Ku70, and Ku80 were verified by immunoblotting with PARP-1 (B) and Ku70 and Ku80 (C) monoclonal antibodies.
    Figure Legend Snippet: Identification of DNA ligase III-associated proteins by affinity chromatography. A HeLa nuclear extract was fractionated by using a DNA ligase III affinity chromatography column as described in Materials and Methods. (A) Proteins in comparable fractions eluted with 0.3 M NaCl from the beads liganded by GST and by GST-DNA ligase III (Lig III) were detected by silver staining after separation by SDS-PAGE. The polypeptides indicated were identified by MALDI-TOF mass spectrometry. The identities of PARP-1, Ku70, and Ku80 were verified by immunoblotting with PARP-1 (B) and Ku70 and Ku80 (C) monoclonal antibodies.

    Techniques Used: Affinity Chromatography, Affinity Column, Silver Staining, SDS Page, Mass Spectrometry

    9) Product Images from "Members of the Large Maf Transcription Family Regulate Insulin Gene Transcription in Islet ? Cells"

    Article Title: Members of the Large Maf Transcription Family Regulate Insulin Gene Transcription in Islet ? Cells

    Journal: Molecular and Cellular Biology

    doi: 10.1128/MCB.23.17.6049-6062.2003

    Biochemical isolation of the InsC1/RIPE3b1 DNA-binding subunit. (A) InsC1 affinity chromatography was performed on βTC-3 nuclear extract (NE). The protein composition of each step was determined by SDS-PAGE and silver staining. First affinity, InsC1-(AC)5 Sepharose chromatography; (AC)5, Sepharose chromatography alone; second affinity, InsC1-(AC)5 Sepharose chromatography. (B) The pooled InsC1/RIPE3b1 binding fractions from the second affinity step were subjected to 2-D electrophoresis. The Coomassie blue-stained spots at pH 7.0 and 4.5 (arrow) of approximately 46-kDa were subjected to MALDI-TOF mass spectrometry. (C) βTC-3 nuclear extract (NE) was resolved by 2-D electrophoresis and probed by Western analysis with αMafA.
    Figure Legend Snippet: Biochemical isolation of the InsC1/RIPE3b1 DNA-binding subunit. (A) InsC1 affinity chromatography was performed on βTC-3 nuclear extract (NE). The protein composition of each step was determined by SDS-PAGE and silver staining. First affinity, InsC1-(AC)5 Sepharose chromatography; (AC)5, Sepharose chromatography alone; second affinity, InsC1-(AC)5 Sepharose chromatography. (B) The pooled InsC1/RIPE3b1 binding fractions from the second affinity step were subjected to 2-D electrophoresis. The Coomassie blue-stained spots at pH 7.0 and 4.5 (arrow) of approximately 46-kDa were subjected to MALDI-TOF mass spectrometry. (C) βTC-3 nuclear extract (NE) was resolved by 2-D electrophoresis and probed by Western analysis with αMafA.

    Techniques Used: Isolation, Binding Assay, Affinity Chromatography, SDS Page, Silver Staining, Chromatography, Electrophoresis, Staining, Mass Spectrometry, Western Blot

    10) Product Images from "Sensitive detection and measurement of oligogalacturonides in Arabidopsis"

    Article Title: Sensitive detection and measurement of oligogalacturonides in Arabidopsis

    Journal: Frontiers in Plant Science

    doi: 10.3389/fpls.2015.00258

    The upper panel shows the HPAEC-PAD profiles of fractions extracted from leaves of plants of different age: (A) 3-week-old plants, (B) 7-week-old plants, (C) purified standard oligomer with DP 10, and (D) standard OGs with DP from 3 to 26 . The peak corresponding to the oligomer with DP 10 is indicated with a black dot. (E) MALDI-TOF mass spectrum of the oligomers extracted from 7-week-old plants.
    Figure Legend Snippet: The upper panel shows the HPAEC-PAD profiles of fractions extracted from leaves of plants of different age: (A) 3-week-old plants, (B) 7-week-old plants, (C) purified standard oligomer with DP 10, and (D) standard OGs with DP from 3 to 26 . The peak corresponding to the oligomer with DP 10 is indicated with a black dot. (E) MALDI-TOF mass spectrum of the oligomers extracted from 7-week-old plants.

    Techniques Used: Purification

    11) Product Images from "Optimized Expression of a Thermostable Xylanase from Thermomyces lanuginosus in Pichia pastoris"

    Article Title: Optimized Expression of a Thermostable Xylanase from Thermomyces lanuginosus in Pichia pastoris

    Journal: Applied and Environmental Microbiology

    doi: 10.1128/AEM.69.10.6064-6072.2003

    Purification of XynA and recombinant XynA. Culture media from P. pastoris (a) and T. lanuginosus (b) were processed and applied to a Superdex G-75 HR column as described in Materials and Methods. All fractions were assayed for xylanase activity, and active fractions are in the hatched areas. The active fractions in b were pooled and subjected to another gel filtration step (inset) as described in Materials and Methods. (c) SDS-PAGE of the purified enzymes. Lanes: M, molecular mass markers; 1, purified recombinant XynA (8 μg); 2, purified XynA (8 μg). (d) circular dichroic spectra of recombinant XynA (solid line) and XynA (doted line) were measured as described in Materials and Methods. (e) MALDI-TOF mass spectrum of purified recombinant XynA. Three forms of the protein were detected, and the corresponding peaks, molecular mass, and relative abundance are indicated.
    Figure Legend Snippet: Purification of XynA and recombinant XynA. Culture media from P. pastoris (a) and T. lanuginosus (b) were processed and applied to a Superdex G-75 HR column as described in Materials and Methods. All fractions were assayed for xylanase activity, and active fractions are in the hatched areas. The active fractions in b were pooled and subjected to another gel filtration step (inset) as described in Materials and Methods. (c) SDS-PAGE of the purified enzymes. Lanes: M, molecular mass markers; 1, purified recombinant XynA (8 μg); 2, purified XynA (8 μg). (d) circular dichroic spectra of recombinant XynA (solid line) and XynA (doted line) were measured as described in Materials and Methods. (e) MALDI-TOF mass spectrum of purified recombinant XynA. Three forms of the protein were detected, and the corresponding peaks, molecular mass, and relative abundance are indicated.

    Techniques Used: Purification, Recombinant, Activity Assay, Filtration, SDS Page

    12) Product Images from "Characterization of a Bifidobacterium longum BORI Dipeptidase Belonging to the U34 Family ▿"

    Article Title: Characterization of a Bifidobacterium longum BORI Dipeptidase Belonging to the U34 Family ▿

    Journal:

    doi: 10.1128/AEM.00642-07

    MALDI-TOF MS spectra of native dipeptidase purified from B. longum BORI (A) and His-tagged dipeptidase expressed in E. coli (B).
    Figure Legend Snippet: MALDI-TOF MS spectra of native dipeptidase purified from B. longum BORI (A) and His-tagged dipeptidase expressed in E. coli (B).

    Techniques Used: Mass Spectrometry, Purification

    13) Product Images from "Transport across the Blood-Brain Barrier of Pluronic Leptin"

    Article Title: Transport across the Blood-Brain Barrier of Pluronic Leptin

    Journal: The Journal of Pharmacology and Experimental Therapeutics

    doi: 10.1124/jpet.109.158147

    Mass spectra of leptin and leptin(ss)-P85 conjugates obtained by MALDI-TOF. Leptin or leptin(ss)-P85 was prepared in water or treated with 25 mM dithiothreitol (DTT) for 10 min at 100°C. The sample was then deposited on the plate using sinapinic acid matrix as described under Materials and Methods . The monomer form of leptin has a molecular mass of 16 kDa, whereas leptin(ss)-P85 conjugates include nonmodified leptin and leptin that was attached with 1 up to 3 P85 chains (peak corresponding to 21, 26, and 31 kDa). Only leptin was detected for leptin(ss)-P85 after incubating with DTT.
    Figure Legend Snippet: Mass spectra of leptin and leptin(ss)-P85 conjugates obtained by MALDI-TOF. Leptin or leptin(ss)-P85 was prepared in water or treated with 25 mM dithiothreitol (DTT) for 10 min at 100°C. The sample was then deposited on the plate using sinapinic acid matrix as described under Materials and Methods . The monomer form of leptin has a molecular mass of 16 kDa, whereas leptin(ss)-P85 conjugates include nonmodified leptin and leptin that was attached with 1 up to 3 P85 chains (peak corresponding to 21, 26, and 31 kDa). Only leptin was detected for leptin(ss)-P85 after incubating with DTT.

    Techniques Used:

    14) Product Images from "Differential Regulation of the PanA and PanB Proteasome-Activating Nucleotidase and 20S Proteasomal Proteins of the Haloarchaeon Haloferax volcanii †"

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

    Journal: Journal of Bacteriology

    doi: 10.1128/JB.186.22.7763-7772.2004

    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.
    Figure Legend 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.

    Techniques Used: Sequencing

    15) Product Images from "Heat shock factor 1 over-expression protects against exposure of hydrophobic residues on mutant SOD1 and early mortality in a mouse model of amyotrophic lateral sclerosis"

    Article Title: Heat shock factor 1 over-expression protects against exposure of hydrophobic residues on mutant SOD1 and early mortality in a mouse model of amyotrophic lateral sclerosis

    Journal: Molecular Neurodegeneration

    doi: 10.1186/1750-1326-8-43

    Altered surface hydrophobicity of mutant SOD1 and non-SOD1 proteins in the spinal cords of symptomatic ALS mice. A) Representative 2D gels of wild type transgenic human SOD1 (WT TG, n = 8) and H46R/H48Q (n = 12) with molecular weights (left axis) and isoelectric points (pI, upper axis). Spots that significantly differed from WT TG in hydrophobic ratio are circled and annotated based on the gene names of their accession numbers identified by MALDI-TOF mass spectrometry. B) Enhanced region of 2D gels containing WT SOD1 and H46R/H48Q mutant SOD1 proteins. BisANS fluorescence and corresponding total protein stained with Sypro Ruby are shown. Quantitated SOD1 spots are shown with numbered ellipses and correspond to the quantitated hydrophobic ratio shown in C) . Bars represent the mean hydrophobic ratio +/- standard deviation of 10- 8 mice per group. *p
    Figure Legend Snippet: Altered surface hydrophobicity of mutant SOD1 and non-SOD1 proteins in the spinal cords of symptomatic ALS mice. A) Representative 2D gels of wild type transgenic human SOD1 (WT TG, n = 8) and H46R/H48Q (n = 12) with molecular weights (left axis) and isoelectric points (pI, upper axis). Spots that significantly differed from WT TG in hydrophobic ratio are circled and annotated based on the gene names of their accession numbers identified by MALDI-TOF mass spectrometry. B) Enhanced region of 2D gels containing WT SOD1 and H46R/H48Q mutant SOD1 proteins. BisANS fluorescence and corresponding total protein stained with Sypro Ruby are shown. Quantitated SOD1 spots are shown with numbered ellipses and correspond to the quantitated hydrophobic ratio shown in C) . Bars represent the mean hydrophobic ratio +/- standard deviation of 10- 8 mice per group. *p

    Techniques Used: Mutagenesis, Mouse Assay, Transgenic Assay, Mass Spectrometry, Fluorescence, Staining, Standard Deviation

    16) Product Images from "Chemical validation of molecular mimicry: interaction of cholera toxin with Campylobacter lipooligosaccharides"

    Article Title: Chemical validation of molecular mimicry: interaction of cholera toxin with Campylobacter lipooligosaccharides

    Journal:

    doi: 10.1007/s10719-006-9025-9

    MALDI-TOF mass spectra of LS and LF. a ) obtained from mild acid hydrolysis of LS. b : The DMB-labeled oligosaccharides (see peak B in ) obtained from mild acid hydrolysis of LS. c : LF
    Figure Legend Snippet: MALDI-TOF mass spectra of LS and LF. a ) obtained from mild acid hydrolysis of LS. b : The DMB-labeled oligosaccharides (see peak B in ) obtained from mild acid hydrolysis of LS. c : LF

    Techniques Used: Labeling

    Related Articles

    High Performance Liquid Chromatography:

    Article Title: An Engineered Saccharomyces cerevisiae Strain Binds the Broadly Neutralizing Human Immunodeficiency Virus Type 1 Antibody 2G12 and Elicits Mannose-Specific gp120-Binding Antibodies
    Article Snippet: .. Glycans were permethylated for analysis by matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometry (MS) using a QSTAR hybrid mass spectrometer (Applied Biosystems, Foster City, CA) and derivatized with 2-aminobenzamide (2AB) for normal-phase high-performance liquid chromatography (NP-HPLC) analysis on a Dionex DX-600 HPLC system (Sunnyvale, CA). .. 2AB-derivatized N-linked glycans released from RNase B were used as a standard for HPLC.

    Nucleic Acid Electrophoresis:

    Article Title: Isolation and Biochemical Characterization of Apios Tuber Lectin
    Article Snippet: .. Molecular Mass Determination of ATL The molecular mass of ATL and the subunit structure were determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), size exclusion chromatography, and matrix-assisted laser desorption ionization time of flight (MALDI-TOF) mass spectrometry (Voyager-DETM STR, Applied Biosystems, Foster City, CA, USA). .. SDS-PAGE was performed according to the method of Laemmli [ ] using 15% separating gel in the presence or absence of 2-mercaptoethanol, and protein bands were stained by Coomassie Brilliant Blue R-250.

    Flow Cytometry:

    Article Title: Structure, Antimicrobial Activities and Mode of Interaction with Membranes of Bovel Phylloseptins from the Painted-Belly Leaf Frog, Phyllomedusa sauvagii
    Article Snippet: .. The homogeneity and identity of the synthetic peptide were assessed by matrix-assisted laser desorption/ionization-time of flight (MALDI-TOF) mass spectrometry (Voyager DE-PRO Applied Biosystems) and RP-HPLC on a C18 analytical column (modulocart QS uptisphere 5 ODB, 5 mm, 250×4.6 mm, Interchim) using the above conditions with a flow rate of 0.75 mL/min. .. Circular dichroism spectroscopy The far-ultraviolet circular dichroism (CD) spectra were recorded as described .

    Size-exclusion Chromatography:

    Article Title: Isolation and Biochemical Characterization of Apios Tuber Lectin
    Article Snippet: .. Molecular Mass Determination of ATL The molecular mass of ATL and the subunit structure were determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), size exclusion chromatography, and matrix-assisted laser desorption ionization time of flight (MALDI-TOF) mass spectrometry (Voyager-DETM STR, Applied Biosystems, Foster City, CA, USA). .. SDS-PAGE was performed according to the method of Laemmli [ ] using 15% separating gel in the presence or absence of 2-mercaptoethanol, and protein bands were stained by Coomassie Brilliant Blue R-250.

    Purification:

    Article Title: Binding Partners for the UL11 Tegument Protein of Herpes Simplex Virus Type 1
    Article Snippet: .. The purified peptides were spotted onto a stainless steel plate, overlaid with an alpha-cyanohydroxycinnamic acid (Sigma) matrix, and analyzed by matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometry (MS) with an Applied Biosystems 4700 proteomics analyzer at the core facility at the College of Medicine, The Pennsylvania State University. .. The 10 most abundant peptide fragments on the spectra were identified and further analyzed by tandem MS-MS ion fragment analysis.

    Article Title: Characterization of Amylolysin, a Novel Lantibiotic from Bacillus amyloliquefaciens GA1
    Article Snippet: .. Mass spectrometry The molecular mass of the purified amylolysin was determined by matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometry using a 4700 Proteomics analyzer (Applied Biosystem). .. Purified amylolysin was mixed with an equal volume of α-cyanohydroxycinnamic acid solution (10 mg/ml) and spotted onto the MALDI plate.

    Concentration Assay:

    Article Title: Physical and Functional Interaction between DNA Ligase III? and Poly(ADP-Ribose) Polymerase 1 in DNA Single-Strand Break Repair
    Article Snippet: .. After concentration to 5 μl, an equal volume of 50% acetonitrile-5% formic acid was added, and an aliquot (1 μl) was analyzed by matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometry (Voyager-DE Pro; Applied Biosystems). ..

    Normal Phase Liquid Chromatography:

    Article Title: An Engineered Saccharomyces cerevisiae Strain Binds the Broadly Neutralizing Human Immunodeficiency Virus Type 1 Antibody 2G12 and Elicits Mannose-Specific gp120-Binding Antibodies
    Article Snippet: .. Glycans were permethylated for analysis by matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometry (MS) using a QSTAR hybrid mass spectrometer (Applied Biosystems, Foster City, CA) and derivatized with 2-aminobenzamide (2AB) for normal-phase high-performance liquid chromatography (NP-HPLC) analysis on a Dionex DX-600 HPLC system (Sunnyvale, CA). .. 2AB-derivatized N-linked glycans released from RNase B were used as a standard for HPLC.

    Mass Spectrometry:

    Article Title: Physical and Functional Interaction between DNA Ligase III? and Poly(ADP-Ribose) Polymerase 1 in DNA Single-Strand Break Repair
    Article Snippet: .. After concentration to 5 μl, an equal volume of 50% acetonitrile-5% formic acid was added, and an aliquot (1 μl) was analyzed by matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometry (Voyager-DE Pro; Applied Biosystems). ..

    Article Title: An Engineered Saccharomyces cerevisiae Strain Binds the Broadly Neutralizing Human Immunodeficiency Virus Type 1 Antibody 2G12 and Elicits Mannose-Specific gp120-Binding Antibodies
    Article Snippet: .. Glycans were permethylated for analysis by matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometry (MS) using a QSTAR hybrid mass spectrometer (Applied Biosystems, Foster City, CA) and derivatized with 2-aminobenzamide (2AB) for normal-phase high-performance liquid chromatography (NP-HPLC) analysis on a Dionex DX-600 HPLC system (Sunnyvale, CA). .. 2AB-derivatized N-linked glycans released from RNase B were used as a standard for HPLC.

    Article Title: Isolation and Biochemical Characterization of Apios Tuber Lectin
    Article Snippet: .. Molecular Mass Determination of ATL The molecular mass of ATL and the subunit structure were determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), size exclusion chromatography, and matrix-assisted laser desorption ionization time of flight (MALDI-TOF) mass spectrometry (Voyager-DETM STR, Applied Biosystems, Foster City, CA, USA). .. SDS-PAGE was performed according to the method of Laemmli [ ] using 15% separating gel in the presence or absence of 2-mercaptoethanol, and protein bands were stained by Coomassie Brilliant Blue R-250.

    Article Title: Binding Partners for the UL11 Tegument Protein of Herpes Simplex Virus Type 1
    Article Snippet: .. The purified peptides were spotted onto a stainless steel plate, overlaid with an alpha-cyanohydroxycinnamic acid (Sigma) matrix, and analyzed by matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometry (MS) with an Applied Biosystems 4700 proteomics analyzer at the core facility at the College of Medicine, The Pennsylvania State University. .. The 10 most abundant peptide fragments on the spectra were identified and further analyzed by tandem MS-MS ion fragment analysis.

    Article Title: Characterization of Amylolysin, a Novel Lantibiotic from Bacillus amyloliquefaciens GA1
    Article Snippet: .. Mass spectrometry The molecular mass of the purified amylolysin was determined by matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometry using a 4700 Proteomics analyzer (Applied Biosystem). .. Purified amylolysin was mixed with an equal volume of α-cyanohydroxycinnamic acid solution (10 mg/ml) and spotted onto the MALDI plate.

    Article Title: Structure, Antimicrobial Activities and Mode of Interaction with Membranes of Bovel Phylloseptins from the Painted-Belly Leaf Frog, Phyllomedusa sauvagii
    Article Snippet: .. The homogeneity and identity of the synthetic peptide were assessed by matrix-assisted laser desorption/ionization-time of flight (MALDI-TOF) mass spectrometry (Voyager DE-PRO Applied Biosystems) and RP-HPLC on a C18 analytical column (modulocart QS uptisphere 5 ODB, 5 mm, 250×4.6 mm, Interchim) using the above conditions with a flow rate of 0.75 mL/min. .. Circular dichroism spectroscopy The far-ultraviolet circular dichroism (CD) spectra were recorded as described .

    Article Title: Cationized liposomal keto-mycolic acids isolated from Mycobacterium bovis bacillus Calmette-Guérin induce antitumor immunity in a syngeneic murine bladder cancer model
    Article Snippet: .. Mass spectrometric analysis of MA subclasses The molecular weight of each MA methylester was determined by matrix-assisted laser desorption/ionization-time of flight (MALDI-TOF) mass spectrometry on a Voyager DE-STR workstation (Applied Biosystems, Foster City, CA) using 2.4-dihydroxybenzoic acid (2.5-DHB) as a matrix, as reported previously [ ]. ..

    Article Title: Synthesis of Maleimide-End Functionalized Star Polymers and Multimeric Protein-Polymer Conjugates
    Article Snippet: .. Matrix-assisted laser desorption/ionization time of flight (MALDI-TOF) mass spectrometry was performed on an Applied Biosystems Voyager-DE STR and operated in linear mode with an external calibration. ..

    SDS Page:

    Article Title: Isolation and Biochemical Characterization of Apios Tuber Lectin
    Article Snippet: .. Molecular Mass Determination of ATL The molecular mass of ATL and the subunit structure were determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), size exclusion chromatography, and matrix-assisted laser desorption ionization time of flight (MALDI-TOF) mass spectrometry (Voyager-DETM STR, Applied Biosystems, Foster City, CA, USA). .. SDS-PAGE was performed according to the method of Laemmli [ ] using 15% separating gel in the presence or absence of 2-mercaptoethanol, and protein bands were stained by Coomassie Brilliant Blue R-250.

    Molecular Weight:

    Article Title: Cationized liposomal keto-mycolic acids isolated from Mycobacterium bovis bacillus Calmette-Guérin induce antitumor immunity in a syngeneic murine bladder cancer model
    Article Snippet: .. Mass spectrometric analysis of MA subclasses The molecular weight of each MA methylester was determined by matrix-assisted laser desorption/ionization-time of flight (MALDI-TOF) mass spectrometry on a Voyager DE-STR workstation (Applied Biosystems, Foster City, CA) using 2.4-dihydroxybenzoic acid (2.5-DHB) as a matrix, as reported previously [ ]. ..

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  • 90
    Thermo Fisher flight maldi tof mass spectrometry uv irradiated
    Representative <t>MALDI-TOF</t> spectra of trypsin-digested samples of γS-WT and γS-G18V after UV-A irradiation. Mass fragments were identified by manual comparison of mass-to-charge ratio peaks to the theoretical peaks and isotopic mass distributions from MS-Digest ( http://prospector.ucsf.edu , in the public domain). Additional mass fragments corresponding to identifiable molecular weight changes are labeled with the specific mass difference, that is, m + 16. Top : The γS-WT spectrum is shown with selected fragments annotated. Insets A and B display the observed cases of m + 4 peaks in matched fragments containing a Trp residue. An m + 4 mass difference matches a Trp-to-Kyn PTM. The masses for each peak are labeled as m Trp and m Kyn . Bottom : The γS-G18V distribution is shown with annotations indicating each of the observed peaks matching an MS-Digest fragment. Kyn, kynurenine.
    Flight Maldi Tof Mass Spectrometry Uv Irradiated, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher matrix assisted laser desorption ionization time of flight maldi tof mass spectrometric analysis
    Production of hirudin and a Fab fragment containing synthetic amino acids in BL21(DE3) and B-95.ΔA. (a) <t>MALDI-TOF</t> analyses of the recombinant HV1 products from the gene with TAG at position 63. The products were from the growth medium (left) and the cytoplasm (right) of BL21(DE3) and B-95.ΔAΔ fabR . The calculated masses (m/z) of the full-length HV1 with and without O -sulfation are 7050.5 and 6970.5, respectively, for [M+H] + . Note that sulfotyrosine can easily be deacylated in this matrix. The calculated mass (m/z) of the truncated HV1 with translation terminated at UAG is 6566.1 for [M+H] + . (b) Fab fragments produced in BL21(DE3) and B-95.ΔA. The purified products and those subsequently labeled with a fluorescent probe were fractionated on NuPAGE gels (in the upper and lower gels, respectively). Fluorescence was detected using an LAS4010 image analyzer. The labeled products correspond to the heavy chain. “WT” and “Am” indicate the products expressed from genes with and without an in-frame TAG, respectively. The figures indicate the yields of the products (mg/l). (c) The Fab fragment from B-95.ΔA, labeled and then purified by protein-G column chromatography, was analyzed by electrophoresis on a NuPAGE gel. (d) Fab fragments containing three 4-azidophenylalanines at the positions marked with “Am” were synthesized in BL21(DE3) (“RF-1+”) and B-95.ΔA (“RF-1−”), and then were analyzed by electrophoresis on a NuPAGE gel. The figures at the bottom of the gel indicate relative yields for the variants. (e) The Fab fragments containing three 4-azidophenylalanines at the positions marked with “Am” were synthesized in B-95.ΔA and labeled, followed by a NuPAGE analysis (upper) and fluorescence detection (lower). The positions corresponding to the Fab fragments labeled at one, two, and three sites are indicated. The size markers in the right-most or left-most lanes in panels b–e indicate 20 and 30 kDa.
    Matrix Assisted Laser Desorption Ionization Time Of Flight Maldi Tof Mass Spectrometric Analysis, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 89/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher time of flight mass spectrometry
    Reverse-phase (RP)-HPLC chromatogram ( a ) and matrix-assisted laser desorption/ionisation, <t>time-of-flight</t> <t>mass</t> <t>spectrometry</t> (MALDI-TOF) mass spectrum ( b ) of a synthetic replicate of peptide RR-18.
    Time Of Flight Mass Spectrometry, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher flight maldi tof tof peptide mass fingerprinting
    Reverse-phase (RP)-HPLC chromatogram ( a ) and matrix-assisted laser desorption/ionisation, <t>time-of-flight</t> <t>mass</t> <t>spectrometry</t> (MALDI-TOF) mass spectrum ( b ) of a synthetic replicate of peptide RR-18.
    Flight Maldi Tof Tof Peptide Mass Fingerprinting, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Representative MALDI-TOF spectra of trypsin-digested samples of γS-WT and γS-G18V after UV-A irradiation. Mass fragments were identified by manual comparison of mass-to-charge ratio peaks to the theoretical peaks and isotopic mass distributions from MS-Digest ( http://prospector.ucsf.edu , in the public domain). Additional mass fragments corresponding to identifiable molecular weight changes are labeled with the specific mass difference, that is, m + 16. Top : The γS-WT spectrum is shown with selected fragments annotated. Insets A and B display the observed cases of m + 4 peaks in matched fragments containing a Trp residue. An m + 4 mass difference matches a Trp-to-Kyn PTM. The masses for each peak are labeled as m Trp and m Kyn . Bottom : The γS-G18V distribution is shown with annotations indicating each of the observed peaks matching an MS-Digest fragment. Kyn, kynurenine.

    Journal: Investigative Ophthalmology & Visual Science

    Article Title: Multiple Aggregation Pathways in Human γS-Crystallin and Its Aggregation-Prone G18V Variant

    doi: 10.1167/iovs.16-20621

    Figure Lengend Snippet: Representative MALDI-TOF spectra of trypsin-digested samples of γS-WT and γS-G18V after UV-A irradiation. Mass fragments were identified by manual comparison of mass-to-charge ratio peaks to the theoretical peaks and isotopic mass distributions from MS-Digest ( http://prospector.ucsf.edu , in the public domain). Additional mass fragments corresponding to identifiable molecular weight changes are labeled with the specific mass difference, that is, m + 16. Top : The γS-WT spectrum is shown with selected fragments annotated. Insets A and B display the observed cases of m + 4 peaks in matched fragments containing a Trp residue. An m + 4 mass difference matches a Trp-to-Kyn PTM. The masses for each peak are labeled as m Trp and m Kyn . Bottom : The γS-G18V distribution is shown with annotations indicating each of the observed peaks matching an MS-Digest fragment. Kyn, kynurenine.

    Article Snippet: Matrix Assisted Laser Desorption Ionization-Time of Flight (MALDI-TOF) Mass Spectrometry UV-irradiated and unexposed proteins were digested using MS Grade Pierce Trypsin Protease (ThermoFischer Scientific, Rockford, IL, USA) at 37°C.

    Techniques: Irradiation, Mass Spectrometry, Molecular Weight, Labeling

    Production of hirudin and a Fab fragment containing synthetic amino acids in BL21(DE3) and B-95.ΔA. (a) MALDI-TOF analyses of the recombinant HV1 products from the gene with TAG at position 63. The products were from the growth medium (left) and the cytoplasm (right) of BL21(DE3) and B-95.ΔAΔ fabR . The calculated masses (m/z) of the full-length HV1 with and without O -sulfation are 7050.5 and 6970.5, respectively, for [M+H] + . Note that sulfotyrosine can easily be deacylated in this matrix. The calculated mass (m/z) of the truncated HV1 with translation terminated at UAG is 6566.1 for [M+H] + . (b) Fab fragments produced in BL21(DE3) and B-95.ΔA. The purified products and those subsequently labeled with a fluorescent probe were fractionated on NuPAGE gels (in the upper and lower gels, respectively). Fluorescence was detected using an LAS4010 image analyzer. The labeled products correspond to the heavy chain. “WT” and “Am” indicate the products expressed from genes with and without an in-frame TAG, respectively. The figures indicate the yields of the products (mg/l). (c) The Fab fragment from B-95.ΔA, labeled and then purified by protein-G column chromatography, was analyzed by electrophoresis on a NuPAGE gel. (d) Fab fragments containing three 4-azidophenylalanines at the positions marked with “Am” were synthesized in BL21(DE3) (“RF-1+”) and B-95.ΔA (“RF-1−”), and then were analyzed by electrophoresis on a NuPAGE gel. The figures at the bottom of the gel indicate relative yields for the variants. (e) The Fab fragments containing three 4-azidophenylalanines at the positions marked with “Am” were synthesized in B-95.ΔA and labeled, followed by a NuPAGE analysis (upper) and fluorescence detection (lower). The positions corresponding to the Fab fragments labeled at one, two, and three sites are indicated. The size markers in the right-most or left-most lanes in panels b–e indicate 20 and 30 kDa.

    Journal: Scientific Reports

    Article Title: Highly reproductive Escherichia coli cells with no specific assignment to the UAG codon

    doi: 10.1038/srep09699

    Figure Lengend Snippet: Production of hirudin and a Fab fragment containing synthetic amino acids in BL21(DE3) and B-95.ΔA. (a) MALDI-TOF analyses of the recombinant HV1 products from the gene with TAG at position 63. The products were from the growth medium (left) and the cytoplasm (right) of BL21(DE3) and B-95.ΔAΔ fabR . The calculated masses (m/z) of the full-length HV1 with and without O -sulfation are 7050.5 and 6970.5, respectively, for [M+H] + . Note that sulfotyrosine can easily be deacylated in this matrix. The calculated mass (m/z) of the truncated HV1 with translation terminated at UAG is 6566.1 for [M+H] + . (b) Fab fragments produced in BL21(DE3) and B-95.ΔA. The purified products and those subsequently labeled with a fluorescent probe were fractionated on NuPAGE gels (in the upper and lower gels, respectively). Fluorescence was detected using an LAS4010 image analyzer. The labeled products correspond to the heavy chain. “WT” and “Am” indicate the products expressed from genes with and without an in-frame TAG, respectively. The figures indicate the yields of the products (mg/l). (c) The Fab fragment from B-95.ΔA, labeled and then purified by protein-G column chromatography, was analyzed by electrophoresis on a NuPAGE gel. (d) Fab fragments containing three 4-azidophenylalanines at the positions marked with “Am” were synthesized in BL21(DE3) (“RF-1+”) and B-95.ΔA (“RF-1−”), and then were analyzed by electrophoresis on a NuPAGE gel. The figures at the bottom of the gel indicate relative yields for the variants. (e) The Fab fragments containing three 4-azidophenylalanines at the positions marked with “Am” were synthesized in B-95.ΔA and labeled, followed by a NuPAGE analysis (upper) and fluorescence detection (lower). The positions corresponding to the Fab fragments labeled at one, two, and three sites are indicated. The size markers in the right-most or left-most lanes in panels b–e indicate 20 and 30 kDa.

    Article Snippet: Matrix-assisted laser desorption ionization time-of-flight (MALDI-TOF) mass spectrometric analysis of recombinant hirudin HV1 was reduced by an incubation in Bond-Breaker TCEP solution (neutral pH) (Thermo Scientific) with TECP at a final concentration of 50 mM at 70°C for 10 min, and then desalted by using a SPE C-TIP(C18) column (Nikkyo Technos, Co., Ltd., Japan), followed by elution in 80% acetonitrile and 0.5% TFA.

    Techniques: Recombinant, Produced, Purification, Labeling, Fluorescence, Column Chromatography, Electrophoresis, Synthesized

    Reverse-phase (RP)-HPLC chromatogram ( a ) and matrix-assisted laser desorption/ionisation, time-of-flight mass spectrometry (MALDI-TOF) mass spectrum ( b ) of a synthetic replicate of peptide RR-18.

    Journal: Biomedicines

    Article Title: Pharmacological Effects of a Novel Bradykinin-Related Peptide (RR-18) from the Skin Secretion of the Hejiang Frog (Ordorrana hejiangensis) on Smooth Muscle

    doi: 10.3390/biomedicines8070225

    Figure Lengend Snippet: Reverse-phase (RP)-HPLC chromatogram ( a ) and matrix-assisted laser desorption/ionisation, time-of-flight mass spectrometry (MALDI-TOF) mass spectrum ( b ) of a synthetic replicate of peptide RR-18.

    Article Snippet: The molecular masses of peptides in the fractions were analysed by matrix-assisted laser desorption/ionisation, time-of-flight mass spectrometry (MALDI-TOF MS) (Thermo Fisher Scientific, San Francisco, CA, USA) using alpha-cyano-4-hydroxycinnamic acid (α-CHCA) (Sigma-Aldrich, Dorset, UK) as the matrix and the putative primary structure of RR-18 was analysed using Sequest algorithm against the self-defined Fasta database in proteome Discoverer 1.0 software (Thermo Fisher Scientific, San Jose, CA, USA).

    Techniques: High Performance Liquid Chromatography, Mass Spectrometry