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  • 99
    Thermo Fisher human genome u133 plus 2 0 array
    Human Genome U133 Plus 2 0 Array, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 3950 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Millipore hplc
    Hplc, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 1217 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Agilent technologies 1100 hplc system
    ( A ) Coomassie blue staining of the purified region-1 and region-2 of mPCSK9 proteins. Region-1 (residues 152–351) and region-2 (residues 249–452) of mouse catalytic domain were cloned and expressed by pET-3a plasmids. The proteins were reduced and purified by a reverse-phase high-performance liquid chromatography <t>(HPLC)</t> on an Agilent <t>1100</t> HPLC system. The purified proteins were analyzed by SDS/PAGE and stained with Coomassie blue. The positions of expressed proteins are shown; ( B ) MALDI mass spectrometry on Region-1. The molecular mass of purified PCSK9 region-1 in fully reduced form (PCSK9-1R). The molecular mass of PCSK9 region-1 as determined by MALDI was 21,201 Da; ( C ) MALDI mass spectrometry on Region-2. The molecular mass of purified PCSK9 region-2 in fully reduced form (PCSK9-2R). The molecular mass of PCSK9 region-2 as determined by MALDI was 21,355 Da.
    1100 Hplc System, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 94/100, based on 8933 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Agilent technologies hplc system
    Total <t>scytonemin</t> content on Chroococcidiopsis strains UAM813(upper graph) and UAM813(lower graph) after irradiation with PAR (plain bars)or UVR+PARR(scratched bars) for 15 days normalized to dry weight quantified by <t>HPLC.</t> Significant differences between light conditions are marked by *** (0.001); ** (0.01); * (0.05).
    Hplc System, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 95/100, based on 11677 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Shimadzu Corporation shimadzu hplc system
    SDS PAGE, Western blot and <t>HPLC</t> analysis of the anti‐human CCR4 immunotoxins. A) SDS PAGE analysis (4–12% NuPAGE, Invitrogen); B) Western blot analysis using a mouse anti‐His mAb (clone#: 4A12E4, Invitrogen); C) Western blot analysis using a mouse anti‐diphtheria toxin mAb (clone# 3B6, Meridian). Lane 1: Protein marker; Lane 2–3: monovalent anti‐human CCR4 immunotoxin [DT390‐scFv (1567), 70.26 kDa]; Lane 4–5: Bivalent anti‐human CCR4 immunotoxin [DT390‐BiscFv (1567), 97.57 kDa]; Lane 5–6: single‐chain foldback diabody anti‐human CCR4 immunotoxin (96.31 kDa). D–F) HPLC analysis with <t>Shimadzu</t> HPLC system using Superdex 200 size‐exclusion column, 10/300 GL (GE healthcare, Cat#: 17‐5175‐01): D) monovalent anti‐human CCR4 immunotoxin [DT390‐scFv (1567)]; E) bivalent anti‐human CCR4 immunotoxin [DT390‐BiscFv (1567)]; F) single‐chain fold‐back diabbody anti‐human CCR4 immunotoxin.
    Shimadzu Hplc System, supplied by Shimadzu Corporation, used in various techniques. Bioz Stars score: 95/100, based on 5808 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Agilent technologies 1200 hplc system
    <t>RP-HPLC</t> analysis of 25S rRNA nucleosides from rrp8–G209R and rrp8–G209A mutant cells. After sucrose gradient centrifugation, 60S subunits were collected with the Density Gradient Fractionation System (Teledyne Isco), and 25S rRNA was isolated. The 25S rRNA was digested with nuclease P1 and bacterial alkaline phosphatase (Sigma-Aldrich). Nucleosides from the mutants ( C and D ) together with the respective wild-type strain ( A ) were analysed by RP-HPLC on a Supelcosil LC-18-S HPLC column (25 cm × 4.6 mm, 5 μm) equipped with a pre-column (4.6 × 20 mm) at 30°C on an Agilent <t>1200</t> HPLC system. ( B ) Estimation of m 1 A peak areas in different rrp8 mutants. The m 1 A peak areas detected in the RP-HPLC analysis of the corresponding strain were estimated using the Agilent ChemStation software. The value for the wild-type was set to 100%.
    1200 Hplc System, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 94/100, based on 7505 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Waters Corporation hplc system
    Effect of hypercholesterolemia on striatal dopamine level in Parkinsonian mice. Mice were sacrificed by decapitation on the seventh day following the first dose of MPTP. Striatal dopamine content was analyzed by <t>HPLC-ECD</t> system. Hypercholesterolemia exaggerates striatal dopamine depletion in Parkinsonian mice. The results are given as mean ± S.E.M. *p ≤ 0.05 as compared to control (CS) and #p ≤ 0.05 as compared to MPTP alone treated group (n = 6).
    Hplc System, supplied by Waters Corporation, used in various techniques. Bioz Stars score: 95/100, based on 7610 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher ultimate 3000 hplc system
    Effect of hypercholesterolemia on striatal dopamine level in Parkinsonian mice. Mice were sacrificed by decapitation on the seventh day following the first dose of MPTP. Striatal dopamine content was analyzed by <t>HPLC-ECD</t> system. Hypercholesterolemia exaggerates striatal dopamine depletion in Parkinsonian mice. The results are given as mean ± S.E.M. *p ≤ 0.05 as compared to control (CS) and #p ≤ 0.05 as compared to MPTP alone treated group (n = 6).
    Ultimate 3000 Hplc System, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 4570 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher hplc
    Effect of hypercholesterolemia on striatal dopamine level in Parkinsonian mice. Mice were sacrificed by decapitation on the seventh day following the first dose of MPTP. Striatal dopamine content was analyzed by <t>HPLC-ECD</t> system. Hypercholesterolemia exaggerates striatal dopamine depletion in Parkinsonian mice. The results are given as mean ± S.E.M. *p ≤ 0.05 as compared to control (CS) and #p ≤ 0.05 as compared to MPTP alone treated group (n = 6).
    Hplc, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 4818 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Waters Corporation rp hplc
    Figure 1. <t>RP-HPLC</t> chromatogram of ( A ) Cell culture harvest and ( B ) <t>mAb1</t> Protein A intermediate.
    Rp Hplc, supplied by Waters Corporation, used in various techniques. Bioz Stars score: 94/100, based on 2080 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore hplc grade
    Figure 1. <t>RP-HPLC</t> chromatogram of ( A ) Cell culture harvest and ( B ) <t>mAb1</t> Protein A intermediate.
    Hplc Grade, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 2238 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Phenomenex rp hplc
    ( a ) Reverse phase high performance liquid chromatography <t>(HPLC)</t> chromatogram of skin secretion of Phyllomedusa camba monitored at 214 nm. The arrow indicated the retention time of <t>PSN-PC;</t> ( b ) Tandem mass (MS/MS) fragmentation spectrum of PSN-PC; ( c ) Predicted singly-charged b ions and y ions arising from MS/MS fragmentation. The observed b- and y-ions were indicated in blue and red typefaces.
    Rp Hplc, supplied by Phenomenex, used in various techniques. Bioz Stars score: 94/100, based on 2382 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Agilent technologies rp hplc
    Solid-phase purification of the phosphorothioate DNA sequence 10b . <t>RP-HPLC</t> analysis of solid-phase-purified 12b that was released from the support 11b . Inset: Purity analysis of the solid-phase-purified 12b by <t>PAGE.</t> Abbreviation: BP, bromophenol blue dye.
    Rp Hplc, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 94/100, based on 2093 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Fisher Scientific hplc grade
    Solid-phase purification of the phosphorothioate DNA sequence 10b . <t>RP-HPLC</t> analysis of solid-phase-purified 12b that was released from the support 11b . Inset: Purity analysis of the solid-phase-purified 12b by <t>PAGE.</t> Abbreviation: BP, bromophenol blue dye.
    Hplc Grade, supplied by Fisher Scientific, used in various techniques. Bioz Stars score: 92/100, based on 1820 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    ( A ) Coomassie blue staining of the purified region-1 and region-2 of mPCSK9 proteins. Region-1 (residues 152–351) and region-2 (residues 249–452) of mouse catalytic domain were cloned and expressed by pET-3a plasmids. The proteins were reduced and purified by a reverse-phase high-performance liquid chromatography (HPLC) on an Agilent 1100 HPLC system. The purified proteins were analyzed by SDS/PAGE and stained with Coomassie blue. The positions of expressed proteins are shown; ( B ) MALDI mass spectrometry on Region-1. The molecular mass of purified PCSK9 region-1 in fully reduced form (PCSK9-1R). The molecular mass of PCSK9 region-1 as determined by MALDI was 21,201 Da; ( C ) MALDI mass spectrometry on Region-2. The molecular mass of purified PCSK9 region-2 in fully reduced form (PCSK9-2R). The molecular mass of PCSK9 region-2 as determined by MALDI was 21,355 Da.

    Journal: International Journal of Molecular Sciences

    Article Title: Non-Native Conformational Isomers of the Catalytic Domain of PCSK9 Induce an Immune Response, Reduce Lipids and Increase LDL Receptor Levels

    doi: 10.3390/ijms19020640

    Figure Lengend Snippet: ( A ) Coomassie blue staining of the purified region-1 and region-2 of mPCSK9 proteins. Region-1 (residues 152–351) and region-2 (residues 249–452) of mouse catalytic domain were cloned and expressed by pET-3a plasmids. The proteins were reduced and purified by a reverse-phase high-performance liquid chromatography (HPLC) on an Agilent 1100 HPLC system. The purified proteins were analyzed by SDS/PAGE and stained with Coomassie blue. The positions of expressed proteins are shown; ( B ) MALDI mass spectrometry on Region-1. The molecular mass of purified PCSK9 region-1 in fully reduced form (PCSK9-1R). The molecular mass of PCSK9 region-1 as determined by MALDI was 21,201 Da; ( C ) MALDI mass spectrometry on Region-2. The molecular mass of purified PCSK9 region-2 in fully reduced form (PCSK9-2R). The molecular mass of PCSK9 region-2 as determined by MALDI was 21,355 Da.

    Article Snippet: The authors used a reverse-phase high-performance liquid chromatography (HPLC) on an Agilent 1100 HPLC system (Column ZORBAX 3000 SB-C18, 9.4 mm × 25 cm) to purify the proteins.

    Techniques: Staining, Purification, Clone Assay, Positron Emission Tomography, High Performance Liquid Chromatography, SDS Page, Mass Spectrometry

    Reactor set-up for carvone optimisation using RD1 as an inline spectroscopic flow cell. Reagents were pumped using an Agilent 1100 series HPLC pumping module. A Uniqsis FlowSyn was used to heat and cool the 5 mL stainless steel coil reactor. The flow passed onto a stand-alone six-port valve, whereby samples were either passed into a collection vial or passed through RD1 which sat within the DAD compartment of the same Agilent 1100 series HPLC.

    Journal: Beilstein Journal of Organic Chemistry

    Article Title: 3D printed fluidics with embedded analytic functionality for automated reaction optimisation

    doi: 10.3762/bjoc.13.14

    Figure Lengend Snippet: Reactor set-up for carvone optimisation using RD1 as an inline spectroscopic flow cell. Reagents were pumped using an Agilent 1100 series HPLC pumping module. A Uniqsis FlowSyn was used to heat and cool the 5 mL stainless steel coil reactor. The flow passed onto a stand-alone six-port valve, whereby samples were either passed into a collection vial or passed through RD1 which sat within the DAD compartment of the same Agilent 1100 series HPLC.

    Article Snippet: RD2 was therefore designed to match the internal dimensions of the heated column compartment of an Agilent 1100 series HPLC system ( ).

    Techniques: Flow Cytometry, High Performance Liquid Chromatography

    RD1 held in place within the DAD compartment of an Agilent 1100 HPLC.

    Journal: Beilstein Journal of Organic Chemistry

    Article Title: 3D printed fluidics with embedded analytic functionality for automated reaction optimisation

    doi: 10.3762/bjoc.13.14

    Figure Lengend Snippet: RD1 held in place within the DAD compartment of an Agilent 1100 HPLC.

    Article Snippet: RD2 was therefore designed to match the internal dimensions of the heated column compartment of an Agilent 1100 series HPLC system ( ).

    Techniques: High Performance Liquid Chromatography

    aps1 and pgm leaves accumulate WT ADPG content. (A) HPLC-MS/MS detection of ADPG in WT, aps1 and pgm leaves. Upper panels: Total ion chromatograms (TIC) of extracts from the indicated plants in which the selected fragmentation parent ion was 587.8 m/z. Middle panels: Extracted ion chromatograms (EIC) in which the selected ion for fragmentation of the parent ion was 346.1 m/z. Lower panels: Mass spectra (MS2) obtained from fragmentation of parent ion. ADPG was measured using an Agilent 1100 HPLC fitted with a Xbridge C18 column (100×3.0 mm I.D. particle size 3.5 µm) coupled to a MSD-Trap spectrometer (Agilent) (see Materials and Methods for further details). (B) ADPG content in WT, aps1, pgm and aps1/pgm leaves. Plants were simultaneously grown either in soil or solid MS. Leaves from 4-weeks old WT, aps1, pgm and aps1/pgm plants were simultaneously harvested after 10 h of illumination. ADPG was simultaneouly extracted from leaves of WT, aps1, pgm and aps1/pgm plants and content was simultaneously measured by HPLC-MS/MS as described in Materials and Methods . Note that, consistent with [15] , leaves of aps1, pgm and aps1/pgm plants accumulated WT ADPG content. Values represent the mean ±SD of determinations on three independent samples.

    Journal: PLoS ONE

    Article Title: HPLC-MS/MS Analyses Show That the Near-Starchless aps1 and pgm Leaves Accumulate Wild Type Levels of ADPglucose: Further Evidence for the Occurrence of Important ADPglucose Biosynthetic Pathway(s) Alternative to the pPGI-pPGM-AGP Pathway

    doi: 10.1371/journal.pone.0104997

    Figure Lengend Snippet: aps1 and pgm leaves accumulate WT ADPG content. (A) HPLC-MS/MS detection of ADPG in WT, aps1 and pgm leaves. Upper panels: Total ion chromatograms (TIC) of extracts from the indicated plants in which the selected fragmentation parent ion was 587.8 m/z. Middle panels: Extracted ion chromatograms (EIC) in which the selected ion for fragmentation of the parent ion was 346.1 m/z. Lower panels: Mass spectra (MS2) obtained from fragmentation of parent ion. ADPG was measured using an Agilent 1100 HPLC fitted with a Xbridge C18 column (100×3.0 mm I.D. particle size 3.5 µm) coupled to a MSD-Trap spectrometer (Agilent) (see Materials and Methods for further details). (B) ADPG content in WT, aps1, pgm and aps1/pgm leaves. Plants were simultaneously grown either in soil or solid MS. Leaves from 4-weeks old WT, aps1, pgm and aps1/pgm plants were simultaneously harvested after 10 h of illumination. ADPG was simultaneouly extracted from leaves of WT, aps1, pgm and aps1/pgm plants and content was simultaneously measured by HPLC-MS/MS as described in Materials and Methods . Note that, consistent with [15] , leaves of aps1, pgm and aps1/pgm plants accumulated WT ADPG content. Values represent the mean ±SD of determinations on three independent samples.

    Article Snippet: ADPG content in leaves of plants cultured on soil was measured in the Research Support Service at the Public University of Navarra using an Agilent 1100 HPLC fitted with a Xbridge C18 column (100×3.0 mm I.D. particle size 3.5 µm) coupled to a MSD-Trap spectrometer (Agilent).

    Techniques: High Performance Liquid Chromatography, Mass Spectrometry

    Identification of OGP as the molecule unbound from ZP after incubation in oviductal fluid (30 min) and further incubation in TALPp medium (1 h). One hundred ZPs from IVM porcine oocytes were preincubated in bOF (1 ZP/0.5 μl OF) and later in TALPp medium. Lane1 shows the SDS-PAGE electrophoresis under reducing conditions of the TALPp medium. Lane 2 shows the lysate of 100 ZPs after being removed from the medium. The two bands observed in lane 1, of ≈95 and ≈75 kDa, were analyzed on an Agilent 1100 Series HPLC. Five peptides in the 95-kDa band and five peptides in the 75-kDa band corresponding to OGP were identified.

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Oviduct-specific glycoprotein and heparin modulate sperm-zona pellucida interaction during fertilization and contribute to the control of polyspermy

    doi: 10.1073/pnas.0804422105

    Figure Lengend Snippet: Identification of OGP as the molecule unbound from ZP after incubation in oviductal fluid (30 min) and further incubation in TALPp medium (1 h). One hundred ZPs from IVM porcine oocytes were preincubated in bOF (1 ZP/0.5 μl OF) and later in TALPp medium. Lane1 shows the SDS-PAGE electrophoresis under reducing conditions of the TALPp medium. Lane 2 shows the lysate of 100 ZPs after being removed from the medium. The two bands observed in lane 1, of ≈95 and ≈75 kDa, were analyzed on an Agilent 1100 Series HPLC. Five peptides in the 95-kDa band and five peptides in the 75-kDa band corresponding to OGP were identified.

    Article Snippet: These bands were cut and processed for proteomic analysis, which was carried out on an HPLC/MS system consisting of an Agilent 1100 Series HPLC connected to an MSD Trap XCT Plus (Agilent Technologies) using an ESI (electrospray) interface.

    Techniques: Incubation, SDS Page, Electrophoresis, High Performance Liquid Chromatography

    Total scytonemin content on Chroococcidiopsis strains UAM813(upper graph) and UAM813(lower graph) after irradiation with PAR (plain bars)or UVR+PARR(scratched bars) for 15 days normalized to dry weight quantified by HPLC. Significant differences between light conditions are marked by *** (0.001); ** (0.01); * (0.05).

    Journal: bioRxiv

    Article Title: Response of endolithic Chroococcidiopsis strains from the polyextreme Atacama Desert to light radiation

    doi: 10.1101/2020.09.01.278960

    Figure Lengend Snippet: Total scytonemin content on Chroococcidiopsis strains UAM813(upper graph) and UAM813(lower graph) after irradiation with PAR (plain bars)or UVR+PARR(scratched bars) for 15 days normalized to dry weight quantified by HPLC. Significant differences between light conditions are marked by *** (0.001); ** (0.01); * (0.05).

    Article Snippet: Partially purified scytonemin was analyzed using a HPLC system (Agilent Technologies 1200 Series, Photodiode Array).

    Techniques: Irradiation, High Performance Liquid Chromatography

    The HPLC chromatogram and absorption spectra of scytonemin extract of Chroococcidiopsis strains UAM813 (A, C, E) and UAM816 (B, D, F). A and B: The HPLC chromatogram of the reduced (a) and oxidized (b) scytonemin in UAM813 and UAM816. The absorption spectra of the reduced scytonemin of UAM813 (C) and UAM816 (D), and the oxidized scytonemin of UAM813 (E) and UAM816 (F)

    Journal: bioRxiv

    Article Title: Response of endolithic Chroococcidiopsis strains from the polyextreme Atacama Desert to light radiation

    doi: 10.1101/2020.09.01.278960

    Figure Lengend Snippet: The HPLC chromatogram and absorption spectra of scytonemin extract of Chroococcidiopsis strains UAM813 (A, C, E) and UAM816 (B, D, F). A and B: The HPLC chromatogram of the reduced (a) and oxidized (b) scytonemin in UAM813 and UAM816. The absorption spectra of the reduced scytonemin of UAM813 (C) and UAM816 (D), and the oxidized scytonemin of UAM813 (E) and UAM816 (F)

    Article Snippet: Partially purified scytonemin was analyzed using a HPLC system (Agilent Technologies 1200 Series, Photodiode Array).

    Techniques: High Performance Liquid Chromatography

    Overall structures of LmRPH at different states. ( A ) Structure of wild-type LmRPH in complex with RIF, ANP, and Mg 2+ . The AD, RD, and HD are colored lemon, light blue, and orange, respectively. ANP and RIF are shown as sticks and are colored green and magenta, respectively. Mg 2+ is shown as a sphere. ( B ) Gel-filtration profiles of wild-type LmRPH (red) and the G527A (green), G527S (cyan), and G527Y (blue) mutants. ( C ) In vitro catalytic activity of Gly527 mutants detected by HPLC. The reaction time of G527A, G527S, and G527Y is 1 h, and that of wild-type LmRPH is 5 min. Proteins were used at 0.5 mg/mL. ( D ) E . coli growth assay for Gly527 mutants. Bacteria transformed with wild-type LmRPH, vector, G527A, G527S, or G527Y were cultured in solid LB medium complemented with 0, 10, 40, or 80 μg/mL RIF. ( E ) Structure of LmRPH G527Y in apo form. ( F ) Structure of LmRPH G527Y in complex with ANP and Mg 2+ . Color codes in E and F are as A .

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Structural basis of rifampin inactivation by rifampin phosphotransferase

    doi: 10.1073/pnas.1523614113

    Figure Lengend Snippet: Overall structures of LmRPH at different states. ( A ) Structure of wild-type LmRPH in complex with RIF, ANP, and Mg 2+ . The AD, RD, and HD are colored lemon, light blue, and orange, respectively. ANP and RIF are shown as sticks and are colored green and magenta, respectively. Mg 2+ is shown as a sphere. ( B ) Gel-filtration profiles of wild-type LmRPH (red) and the G527A (green), G527S (cyan), and G527Y (blue) mutants. ( C ) In vitro catalytic activity of Gly527 mutants detected by HPLC. The reaction time of G527A, G527S, and G527Y is 1 h, and that of wild-type LmRPH is 5 min. Proteins were used at 0.5 mg/mL. ( D ) E . coli growth assay for Gly527 mutants. Bacteria transformed with wild-type LmRPH, vector, G527A, G527S, or G527Y were cultured in solid LB medium complemented with 0, 10, 40, or 80 μg/mL RIF. ( E ) Structure of LmRPH G527Y in apo form. ( F ) Structure of LmRPH G527Y in complex with ANP and Mg 2+ . Color codes in E and F are as A .

    Article Snippet: To identify the product RIF-P, the C18 column used for HPLC analysis was connected with an Agilent G6520A accurate-mass quadrupole time-of-flight LC-MS system (LC1200/MS Q-TOF6520).

    Techniques: Aqueous Normal-phase Chromatography, Filtration, In Vitro, Activity Assay, High Performance Liquid Chromatography, Growth Assay, Transformation Assay, Plasmid Preparation, Cell Culture

    Activity of LmRPH. ( A ) In vitro LmRPH reaction products analyzed by HPLC with the RIF detection program. ( B ) Identification of the two peaks in A by LC-MS. ( Left ) Peak 1. ( Right ) Peak 2. ( C ) The samples in A were analyzed by HPLC with a nucleotide-detection program. ( D ) E . coli growth assay. Bacteria transformed with LmRPH or vector were cultured in solid LB medium complemented with 0, 10, 100, or 1,000 μg/mL RIF.

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Structural basis of rifampin inactivation by rifampin phosphotransferase

    doi: 10.1073/pnas.1523614113

    Figure Lengend Snippet: Activity of LmRPH. ( A ) In vitro LmRPH reaction products analyzed by HPLC with the RIF detection program. ( B ) Identification of the two peaks in A by LC-MS. ( Left ) Peak 1. ( Right ) Peak 2. ( C ) The samples in A were analyzed by HPLC with a nucleotide-detection program. ( D ) E . coli growth assay. Bacteria transformed with LmRPH or vector were cultured in solid LB medium complemented with 0, 10, 100, or 1,000 μg/mL RIF.

    Article Snippet: To identify the product RIF-P, the C18 column used for HPLC analysis was connected with an Agilent G6520A accurate-mass quadrupole time-of-flight LC-MS system (LC1200/MS Q-TOF6520).

    Techniques: Activity Assay, In Vitro, High Performance Liquid Chromatography, Liquid Chromatography with Mass Spectroscopy, Growth Assay, Transformation Assay, Plasmid Preparation, Cell Culture

    Catalytic center of RIF phosphorylation. ( A ) Catalytic site of RIF phosphorylation. Residues His825, Lys670, Arg666, and Gln337 and RIF are shown as sticks; the water molecule is shown as a red sphere. Distances between the water molecule and surrounding residues are shown as dashed lines. ( B ) Catalytic site with a modeled RIF-P. Distances between the phosphate group and residues are shown as dashed lines. ( C ) In vitro catalytic activity of H825A, K670A, R666A, and Q337A detected by HPLC. ( D ) E . coli growth assay of the mutants in C. Bacteria transformed with wild-type LmRPH, vector, or mutants were cultured in solid LB medium complemented with 0 or 10 μg/mL RIF. ( E ) Phosphorylation analysis of wild-type LmRPH and the H825A mutant using Phos-tag SDS PAGE. LmRPH-P, phosphorylated LmRPH.

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Structural basis of rifampin inactivation by rifampin phosphotransferase

    doi: 10.1073/pnas.1523614113

    Figure Lengend Snippet: Catalytic center of RIF phosphorylation. ( A ) Catalytic site of RIF phosphorylation. Residues His825, Lys670, Arg666, and Gln337 and RIF are shown as sticks; the water molecule is shown as a red sphere. Distances between the water molecule and surrounding residues are shown as dashed lines. ( B ) Catalytic site with a modeled RIF-P. Distances between the phosphate group and residues are shown as dashed lines. ( C ) In vitro catalytic activity of H825A, K670A, R666A, and Q337A detected by HPLC. ( D ) E . coli growth assay of the mutants in C. Bacteria transformed with wild-type LmRPH, vector, or mutants were cultured in solid LB medium complemented with 0 or 10 μg/mL RIF. ( E ) Phosphorylation analysis of wild-type LmRPH and the H825A mutant using Phos-tag SDS PAGE. LmRPH-P, phosphorylated LmRPH.

    Article Snippet: To identify the product RIF-P, the C18 column used for HPLC analysis was connected with an Agilent G6520A accurate-mass quadrupole time-of-flight LC-MS system (LC1200/MS Q-TOF6520).

    Techniques: In Vitro, Activity Assay, High Performance Liquid Chromatography, Growth Assay, Transformation Assay, Plasmid Preparation, Cell Culture, Mutagenesis, SDS Page

    ATP-binding site. ( A ) ATP-binding affinity of the AD (green isotherm), wild-type LmRPH (blue isotherm), and the G527Y mutant (red isotherm) measured by ITC. ( B ) Conformational changes of the AD induced by HD binding. The LmRPH–AD structure (gray) is superposed with the AD of the LmRPH G527Y –apo structure (lemon). The L13 loop connecting subdomains I and II is highlighted in red. The interaction interfaces between the AD and HD (orange) are shown in zoom-in views, and residues constituting the interface are shown with side chains. ( C ) Conformational changes induced in the AD and HD by ANP binding. The AD (lemon) and HD (orange) of the LmRPH G527Y –apo structure are superposed with those of the LmRPH G527Y -ANP structure (light blue). Structural elements undergoing conformational changes after ANP binding are colored in red. ( D ) Residues constituting the ATP-binding site. ANP (green) and residues (lemon) are shown as sticks, and Mg 2+ is shown as a lemon sphere. Coordination and hydrogen bonds are shown as dashed lines. ( E ) In vitro catalytic activity of ATP-binding site mutants detected by HPLC. The amounts of enzymes used in the assays of the K22A, R117A, E297A, T136A, Q309A, and R311A mutants are 10× those used in assays of wild-type LmRPH. ( F ) E . coli growth assay for ATP-binding site mutants. Bacteria transformed with wild-type LmRPH, vector, or mutants were cultured in solid LB medium complemented with 0, 10, 40, 80, or 320 μg/mL RIF.

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Structural basis of rifampin inactivation by rifampin phosphotransferase

    doi: 10.1073/pnas.1523614113

    Figure Lengend Snippet: ATP-binding site. ( A ) ATP-binding affinity of the AD (green isotherm), wild-type LmRPH (blue isotherm), and the G527Y mutant (red isotherm) measured by ITC. ( B ) Conformational changes of the AD induced by HD binding. The LmRPH–AD structure (gray) is superposed with the AD of the LmRPH G527Y –apo structure (lemon). The L13 loop connecting subdomains I and II is highlighted in red. The interaction interfaces between the AD and HD (orange) are shown in zoom-in views, and residues constituting the interface are shown with side chains. ( C ) Conformational changes induced in the AD and HD by ANP binding. The AD (lemon) and HD (orange) of the LmRPH G527Y –apo structure are superposed with those of the LmRPH G527Y -ANP structure (light blue). Structural elements undergoing conformational changes after ANP binding are colored in red. ( D ) Residues constituting the ATP-binding site. ANP (green) and residues (lemon) are shown as sticks, and Mg 2+ is shown as a lemon sphere. Coordination and hydrogen bonds are shown as dashed lines. ( E ) In vitro catalytic activity of ATP-binding site mutants detected by HPLC. The amounts of enzymes used in the assays of the K22A, R117A, E297A, T136A, Q309A, and R311A mutants are 10× those used in assays of wild-type LmRPH. ( F ) E . coli growth assay for ATP-binding site mutants. Bacteria transformed with wild-type LmRPH, vector, or mutants were cultured in solid LB medium complemented with 0, 10, 40, 80, or 320 μg/mL RIF.

    Article Snippet: To identify the product RIF-P, the C18 column used for HPLC analysis was connected with an Agilent G6520A accurate-mass quadrupole time-of-flight LC-MS system (LC1200/MS Q-TOF6520).

    Techniques: Binding Assay, Mutagenesis, Aqueous Normal-phase Chromatography, In Vitro, Activity Assay, High Performance Liquid Chromatography, Growth Assay, Transformation Assay, Plasmid Preparation, Cell Culture

    SDS PAGE, Western blot and HPLC analysis of the anti‐human CCR4 immunotoxins. A) SDS PAGE analysis (4–12% NuPAGE, Invitrogen); B) Western blot analysis using a mouse anti‐His mAb (clone#: 4A12E4, Invitrogen); C) Western blot analysis using a mouse anti‐diphtheria toxin mAb (clone# 3B6, Meridian). Lane 1: Protein marker; Lane 2–3: monovalent anti‐human CCR4 immunotoxin [DT390‐scFv (1567), 70.26 kDa]; Lane 4–5: Bivalent anti‐human CCR4 immunotoxin [DT390‐BiscFv (1567), 97.57 kDa]; Lane 5–6: single‐chain foldback diabody anti‐human CCR4 immunotoxin (96.31 kDa). D–F) HPLC analysis with Shimadzu HPLC system using Superdex 200 size‐exclusion column, 10/300 GL (GE healthcare, Cat#: 17‐5175‐01): D) monovalent anti‐human CCR4 immunotoxin [DT390‐scFv (1567)]; E) bivalent anti‐human CCR4 immunotoxin [DT390‐BiscFv (1567)]; F) single‐chain fold‐back diabbody anti‐human CCR4 immunotoxin.

    Journal: Molecular Oncology

    Article Title: Diphtheria‐toxin based anti‐human CCR4 immunotoxin for targeting human CCR4+ cells in vivo), Diphtheria-toxin based anti-human CCR4 immunotoxin for targeting human CCR4+ cells in vivo

    doi: 10.1016/j.molonc.2015.04.004

    Figure Lengend Snippet: SDS PAGE, Western blot and HPLC analysis of the anti‐human CCR4 immunotoxins. A) SDS PAGE analysis (4–12% NuPAGE, Invitrogen); B) Western blot analysis using a mouse anti‐His mAb (clone#: 4A12E4, Invitrogen); C) Western blot analysis using a mouse anti‐diphtheria toxin mAb (clone# 3B6, Meridian). Lane 1: Protein marker; Lane 2–3: monovalent anti‐human CCR4 immunotoxin [DT390‐scFv (1567), 70.26 kDa]; Lane 4–5: Bivalent anti‐human CCR4 immunotoxin [DT390‐BiscFv (1567), 97.57 kDa]; Lane 5–6: single‐chain foldback diabody anti‐human CCR4 immunotoxin (96.31 kDa). D–F) HPLC analysis with Shimadzu HPLC system using Superdex 200 size‐exclusion column, 10/300 GL (GE healthcare, Cat#: 17‐5175‐01): D) monovalent anti‐human CCR4 immunotoxin [DT390‐scFv (1567)]; E) bivalent anti‐human CCR4 immunotoxin [DT390‐BiscFv (1567)]; F) single‐chain fold‐back diabbody anti‐human CCR4 immunotoxin.

    Article Snippet: Anti‐human CCR4 immunotoxins were analyzed with Shimadzu HPLC system using Superdex 200 size‐exclusion column, 10/300 GL (GE healthcare, Cat#: 17‐5175‐01).

    Techniques: SDS Page, Western Blot, High Performance Liquid Chromatography, Marker

    Effect of respiration inhibitors on PpIX production and photodynamic therapy. (A-D) KatoIII cells were incubated with 1 mM ALA and 0.1 μM oligomycin, 1 μM rotenone, or 1 μM antimycin for 24 h under atmospheres containing 21% O 2 or 1% O 2 . (A) Intracellular PpIX, (B) intracellular CPIII, (C) extracellular PpIX, and (D) extracellular CPIII were measured using HPLC. Data are expressed as the means ± S.D. from multi-replicated (n = 3) experiments. (E) KatoIII cells were incubated with 0.1 μM oligomycin for 24 h under atmospheres containing 21% O 2 or 1% O 2 . mRNA expression levels of ALAD , HMBS , UROS , UROD , CPOX , PPOX , FECH , PEPT1 , ABCB6 , and ABCG2 were analyzed by quantitative PCR. Data are expressed as the means ± S.D. from multi-replicated (n = 2) experiments. ALAD , aminolevulinic acid dehydrogenase; HMBS , hydroxymethylbilane synthase; UROS , uroporphyrinogen III synthase; UROD , uroporphyrinogen III decarboxylase; CPOX , coproporphyrinogen III oxidase; PPOX , protoporphyrinogen oxidase; FECH , ferrochelatase; PEPT1 , Peptide transporter 1 (F) KatoIII cells were incubated with 1 mM ALA and 0.1 μM Oligomycin for 24 h under atmospheres containing 21% O 2 or 1% O 2 . Exposure to light was performed under an atmosphere containing 21% O 2 and cell viability was measured using the MTT assay. Data are expressed as the means ± S.D. from multi-replicated (n = 3) experiments.

    Journal: PLoS ONE

    Article Title: Oxygen Availability for Porphyrin Biosynthesis Enzymes Determines the Production of Protoporphyrin IX (PpIX) during Hypoxia

    doi: 10.1371/journal.pone.0146026

    Figure Lengend Snippet: Effect of respiration inhibitors on PpIX production and photodynamic therapy. (A-D) KatoIII cells were incubated with 1 mM ALA and 0.1 μM oligomycin, 1 μM rotenone, or 1 μM antimycin for 24 h under atmospheres containing 21% O 2 or 1% O 2 . (A) Intracellular PpIX, (B) intracellular CPIII, (C) extracellular PpIX, and (D) extracellular CPIII were measured using HPLC. Data are expressed as the means ± S.D. from multi-replicated (n = 3) experiments. (E) KatoIII cells were incubated with 0.1 μM oligomycin for 24 h under atmospheres containing 21% O 2 or 1% O 2 . mRNA expression levels of ALAD , HMBS , UROS , UROD , CPOX , PPOX , FECH , PEPT1 , ABCB6 , and ABCG2 were analyzed by quantitative PCR. Data are expressed as the means ± S.D. from multi-replicated (n = 2) experiments. ALAD , aminolevulinic acid dehydrogenase; HMBS , hydroxymethylbilane synthase; UROS , uroporphyrinogen III synthase; UROD , uroporphyrinogen III decarboxylase; CPOX , coproporphyrinogen III oxidase; PPOX , protoporphyrinogen oxidase; FECH , ferrochelatase; PEPT1 , Peptide transporter 1 (F) KatoIII cells were incubated with 1 mM ALA and 0.1 μM Oligomycin for 24 h under atmospheres containing 21% O 2 or 1% O 2 . Exposure to light was performed under an atmosphere containing 21% O 2 and cell viability was measured using the MTT assay. Data are expressed as the means ± S.D. from multi-replicated (n = 3) experiments.

    Article Snippet: Briefly, PpIX and CPIII were separated using an HPLC system (Prominence, Shimadzu, Kyoto, Japan) equipped with a reversed-phase C18 Column (CAPCELL PAK, C18, SG300, 5 μm, 4.6 mm × 250 mm, Shiseido Co., Ltd., Tokyo, Japan).

    Techniques: Incubation, High Performance Liquid Chromatography, Expressing, Real-time Polymerase Chain Reaction, MTT Assay

    Transcriptional regulation is not associated with the alteration of porphyrin biosynthesis during hypoxia. (A) MKN45, KatoIII, and MKN74 cells were incubated for 24 h under atmospheres containing 21% O 2 or 1% O 2 . mRNA expression levels of ALAD , HMBS , UROS , UROD , CPOX , PPOX , FECH , PEPT1 , ABCB6 , and ABCG2 in each cell line were analyzed by quantitative PCR. Data are expressed as the means ± S.D. from multi-replicated (n = 2) experiments. ALAD , aminolevulinic acid dehydrogenase; HMBS , hydroxymethylbilane synthase; UROS , uroporphyrinogen III synthase; UROD , uroporphyrinogen III decarboxylase; CPOX , coproporphyrinogen III oxidase; PPOX , protoporphyrinogen oxidase; FECH , ferrochelatase; PEPT1 , Peptide transporter 1 (B) KatoIII cells were incubated with 100 μM CoCl 2 , 100 μM deferoxamine (DFO), or 1 mM dimethyloxaloglycine (DMOG) for 24 h under atmospheres containing 21% O 2 or 1% O 2 . Immunoblots were carried out using antibodies against HIF-1α and actin. (C-F) KatoIII cells were incubated with 1 mM ALA and 100 μM CoCl 2 , 100 μM DFO, or 1 mM DMOG for 24 h under atmospheres containing 21% O 2 or 1% O 2 . (C) Intracellular PpIX, (D) intracellular CPIII, (E) extracellular PpIX and (F) extracellular CPIII were measured using HPLC. (G-J) KatoIII cells were incubated with 1 mM ALA and 10 μg/mL cyclohexamide. (G) Intracellular PpIX, (H) intracellular CPIII, (I) extracellular PpIX and (J) extracellular CPIII were measured using HPLC. Data are expressed as the means ± S.D. from multi-replicated (n = 3) experiments.

    Journal: PLoS ONE

    Article Title: Oxygen Availability for Porphyrin Biosynthesis Enzymes Determines the Production of Protoporphyrin IX (PpIX) during Hypoxia

    doi: 10.1371/journal.pone.0146026

    Figure Lengend Snippet: Transcriptional regulation is not associated with the alteration of porphyrin biosynthesis during hypoxia. (A) MKN45, KatoIII, and MKN74 cells were incubated for 24 h under atmospheres containing 21% O 2 or 1% O 2 . mRNA expression levels of ALAD , HMBS , UROS , UROD , CPOX , PPOX , FECH , PEPT1 , ABCB6 , and ABCG2 in each cell line were analyzed by quantitative PCR. Data are expressed as the means ± S.D. from multi-replicated (n = 2) experiments. ALAD , aminolevulinic acid dehydrogenase; HMBS , hydroxymethylbilane synthase; UROS , uroporphyrinogen III synthase; UROD , uroporphyrinogen III decarboxylase; CPOX , coproporphyrinogen III oxidase; PPOX , protoporphyrinogen oxidase; FECH , ferrochelatase; PEPT1 , Peptide transporter 1 (B) KatoIII cells were incubated with 100 μM CoCl 2 , 100 μM deferoxamine (DFO), or 1 mM dimethyloxaloglycine (DMOG) for 24 h under atmospheres containing 21% O 2 or 1% O 2 . Immunoblots were carried out using antibodies against HIF-1α and actin. (C-F) KatoIII cells were incubated with 1 mM ALA and 100 μM CoCl 2 , 100 μM DFO, or 1 mM DMOG for 24 h under atmospheres containing 21% O 2 or 1% O 2 . (C) Intracellular PpIX, (D) intracellular CPIII, (E) extracellular PpIX and (F) extracellular CPIII were measured using HPLC. (G-J) KatoIII cells were incubated with 1 mM ALA and 10 μg/mL cyclohexamide. (G) Intracellular PpIX, (H) intracellular CPIII, (I) extracellular PpIX and (J) extracellular CPIII were measured using HPLC. Data are expressed as the means ± S.D. from multi-replicated (n = 3) experiments.

    Article Snippet: Briefly, PpIX and CPIII were separated using an HPLC system (Prominence, Shimadzu, Kyoto, Japan) equipped with a reversed-phase C18 Column (CAPCELL PAK, C18, SG300, 5 μm, 4.6 mm × 250 mm, Shiseido Co., Ltd., Tokyo, Japan).

    Techniques: Incubation, Expressing, Real-time Polymerase Chain Reaction, Western Blot, High Performance Liquid Chromatography

    Generality of PpIX reduction and CPIII excretion after ALA administration under hypoxic conditions. (A-D) Each cell line was incubated with 1 mM ALA for 24 h under atmospheres containing 21% O 2 or 1% O 2 . (A) Intracellular PpIX, (B) intracellular CPIII, (C) extracellular PpIX, and (D) extracellular CPIII were measured using HPLC. Data are expressed as the means ± S.D. from multi-replicated (n = 3) experiments.

    Journal: PLoS ONE

    Article Title: Oxygen Availability for Porphyrin Biosynthesis Enzymes Determines the Production of Protoporphyrin IX (PpIX) during Hypoxia

    doi: 10.1371/journal.pone.0146026

    Figure Lengend Snippet: Generality of PpIX reduction and CPIII excretion after ALA administration under hypoxic conditions. (A-D) Each cell line was incubated with 1 mM ALA for 24 h under atmospheres containing 21% O 2 or 1% O 2 . (A) Intracellular PpIX, (B) intracellular CPIII, (C) extracellular PpIX, and (D) extracellular CPIII were measured using HPLC. Data are expressed as the means ± S.D. from multi-replicated (n = 3) experiments.

    Article Snippet: Briefly, PpIX and CPIII were separated using an HPLC system (Prominence, Shimadzu, Kyoto, Japan) equipped with a reversed-phase C18 Column (CAPCELL PAK, C18, SG300, 5 μm, 4.6 mm × 250 mm, Shiseido Co., Ltd., Tokyo, Japan).

    Techniques: Incubation, High Performance Liquid Chromatography

    Oxygen dependence of PpIX reduction and CPIII excretion under hypoxic conditions. (A-D) KatoIII gastric cancer cells were incubated with 1 mM ALA for 24 h under atmospheres containing 21%, 10%, 7.5%, 5%, 2.5%, or 1% O 2 . (A) Intracellular PpIX, (B) intracellular CPIII, (C) extracellular PpIX, and (D) extracellular CPIII were measured using HPLC. Data are expressed as the means ± S.D. from multi-replicated (n = 3) experiments.

    Journal: PLoS ONE

    Article Title: Oxygen Availability for Porphyrin Biosynthesis Enzymes Determines the Production of Protoporphyrin IX (PpIX) during Hypoxia

    doi: 10.1371/journal.pone.0146026

    Figure Lengend Snippet: Oxygen dependence of PpIX reduction and CPIII excretion under hypoxic conditions. (A-D) KatoIII gastric cancer cells were incubated with 1 mM ALA for 24 h under atmospheres containing 21%, 10%, 7.5%, 5%, 2.5%, or 1% O 2 . (A) Intracellular PpIX, (B) intracellular CPIII, (C) extracellular PpIX, and (D) extracellular CPIII were measured using HPLC. Data are expressed as the means ± S.D. from multi-replicated (n = 3) experiments.

    Article Snippet: Briefly, PpIX and CPIII were separated using an HPLC system (Prominence, Shimadzu, Kyoto, Japan) equipped with a reversed-phase C18 Column (CAPCELL PAK, C18, SG300, 5 μm, 4.6 mm × 250 mm, Shiseido Co., Ltd., Tokyo, Japan).

    Techniques: Incubation, High Performance Liquid Chromatography

    Mitochondrial PpIX production was reduced under hypoxic conditions. (A) KatoIII mitochondria were isolated using extraction buffer. Immunoblots were carried out using antibodies against HSP90 and COX IV-1. (B) Mitochondrial PpIX production was measured using isolated mitochondria and CPgenIII-containing medium. CPgenIII-containing medium was prepared by incubating KatoIII cells with 1 mM ALA for 24 h under an atmosphere containing 0.1% O2. CPgenIII-containing medium were added to isolated mitochondria and the mixtures were incubated for 12 h under atmospheres containing 21% O2 or 0.1% O2. PpIX was measured using HPLC. Data are expressed as the means ± S.D. from multi-replicated (n = 3) experiments.

    Journal: PLoS ONE

    Article Title: Oxygen Availability for Porphyrin Biosynthesis Enzymes Determines the Production of Protoporphyrin IX (PpIX) during Hypoxia

    doi: 10.1371/journal.pone.0146026

    Figure Lengend Snippet: Mitochondrial PpIX production was reduced under hypoxic conditions. (A) KatoIII mitochondria were isolated using extraction buffer. Immunoblots were carried out using antibodies against HSP90 and COX IV-1. (B) Mitochondrial PpIX production was measured using isolated mitochondria and CPgenIII-containing medium. CPgenIII-containing medium was prepared by incubating KatoIII cells with 1 mM ALA for 24 h under an atmosphere containing 0.1% O2. CPgenIII-containing medium were added to isolated mitochondria and the mixtures were incubated for 12 h under atmospheres containing 21% O2 or 0.1% O2. PpIX was measured using HPLC. Data are expressed as the means ± S.D. from multi-replicated (n = 3) experiments.

    Article Snippet: Briefly, PpIX and CPIII were separated using an HPLC system (Prominence, Shimadzu, Kyoto, Japan) equipped with a reversed-phase C18 Column (CAPCELL PAK, C18, SG300, 5 μm, 4.6 mm × 250 mm, Shiseido Co., Ltd., Tokyo, Japan).

    Techniques: Isolation, Western Blot, Incubation, High Performance Liquid Chromatography

    Average standard calibration curve ( n = 3) for urinary rebamipide determination at (A) 50–10,000 ng/mL and (B) 10,000–50,000 ng/mL. Each point represents urinary rebamipide detection under fluorescence HPLC set at 320 excitation and 380 emission. Also shown are the slope and y -intercept values used for determination of sample concentrations.

    Journal: MethodsX

    Article Title: A simple high performance liquid chromatography method for determination of rebamipide in rat urine

    doi: 10.1016/j.mex.2014.06.002

    Figure Lengend Snippet: Average standard calibration curve ( n = 3) for urinary rebamipide determination at (A) 50–10,000 ng/mL and (B) 10,000–50,000 ng/mL. Each point represents urinary rebamipide detection under fluorescence HPLC set at 320 excitation and 380 emission. Also shown are the slope and y -intercept values used for determination of sample concentrations.

    Article Snippet: Analysis of rebamipide concentrations in the urine involved preparation of rebamipide stock solution, development of low and high linear standard calibration curves to compensate for altered rebamipide concentrations noted in urine samples, use of acetonitrile and hydrochloric acid for urinary rebamipide extraction, and HPLC analysis of rebamipide using a Shimadzu HPLC system.

    Techniques: Fluorescence, High Performance Liquid Chromatography

    Representative HPLC chromatogram of (A) rat urine spiked with 10,000 ng/mL rebamipide and (B) rat urine spiked with 5000 ng/mL rebamipide.

    Journal: MethodsX

    Article Title: A simple high performance liquid chromatography method for determination of rebamipide in rat urine

    doi: 10.1016/j.mex.2014.06.002

    Figure Lengend Snippet: Representative HPLC chromatogram of (A) rat urine spiked with 10,000 ng/mL rebamipide and (B) rat urine spiked with 5000 ng/mL rebamipide.

    Article Snippet: Analysis of rebamipide concentrations in the urine involved preparation of rebamipide stock solution, development of low and high linear standard calibration curves to compensate for altered rebamipide concentrations noted in urine samples, use of acetonitrile and hydrochloric acid for urinary rebamipide extraction, and HPLC analysis of rebamipide using a Shimadzu HPLC system.

    Techniques: High Performance Liquid Chromatography

    Representative HPLC chromatogram of urine sample obtained from a rat dosed with rebamipide.

    Journal: MethodsX

    Article Title: A simple high performance liquid chromatography method for determination of rebamipide in rat urine

    doi: 10.1016/j.mex.2014.06.002

    Figure Lengend Snippet: Representative HPLC chromatogram of urine sample obtained from a rat dosed with rebamipide.

    Article Snippet: Analysis of rebamipide concentrations in the urine involved preparation of rebamipide stock solution, development of low and high linear standard calibration curves to compensate for altered rebamipide concentrations noted in urine samples, use of acetonitrile and hydrochloric acid for urinary rebamipide extraction, and HPLC analysis of rebamipide using a Shimadzu HPLC system.

    Techniques: High Performance Liquid Chromatography

    RP-HPLC analysis of 25S rRNA nucleosides from rrp8–G209R and rrp8–G209A mutant cells. After sucrose gradient centrifugation, 60S subunits were collected with the Density Gradient Fractionation System (Teledyne Isco), and 25S rRNA was isolated. The 25S rRNA was digested with nuclease P1 and bacterial alkaline phosphatase (Sigma-Aldrich). Nucleosides from the mutants ( C and D ) together with the respective wild-type strain ( A ) were analysed by RP-HPLC on a Supelcosil LC-18-S HPLC column (25 cm × 4.6 mm, 5 μm) equipped with a pre-column (4.6 × 20 mm) at 30°C on an Agilent 1200 HPLC system. ( B ) Estimation of m 1 A peak areas in different rrp8 mutants. The m 1 A peak areas detected in the RP-HPLC analysis of the corresponding strain were estimated using the Agilent ChemStation software. The value for the wild-type was set to 100%.

    Journal: Nucleic Acids Research

    Article Title: Yeast Rrp8p, a novel methyltransferase responsible for m1A 645 base modification of 25S rRNA

    doi: 10.1093/nar/gks1102

    Figure Lengend Snippet: RP-HPLC analysis of 25S rRNA nucleosides from rrp8–G209R and rrp8–G209A mutant cells. After sucrose gradient centrifugation, 60S subunits were collected with the Density Gradient Fractionation System (Teledyne Isco), and 25S rRNA was isolated. The 25S rRNA was digested with nuclease P1 and bacterial alkaline phosphatase (Sigma-Aldrich). Nucleosides from the mutants ( C and D ) together with the respective wild-type strain ( A ) were analysed by RP-HPLC on a Supelcosil LC-18-S HPLC column (25 cm × 4.6 mm, 5 μm) equipped with a pre-column (4.6 × 20 mm) at 30°C on an Agilent 1200 HPLC system. ( B ) Estimation of m 1 A peak areas in different rrp8 mutants. The m 1 A peak areas detected in the RP-HPLC analysis of the corresponding strain were estimated using the Agilent ChemStation software. The value for the wild-type was set to 100%.

    Article Snippet: Nucleosides were analysed by RP-HPLC on a Supelcosil LC-18-S HPLC column (25 cm × 4.6 mm, 5 µm) equipped with a pre-column (4.6 × 20 mm) at 30°C on an Agilent 1200 HPLC system.

    Techniques: High Performance Liquid Chromatography, Mutagenesis, Gradient Centrifugation, Fractionation, Isolation, Software

    RP-HPLC analysis of mung bean digested RNA fragments. Specific sequences of the 25S rRNA from wild-type ( A and C ) and the rrp8 -_ C mutant ( B and D ), corresponding to Helix 25.1 and Helix 65, respectively, were isolated by hybridization to complementary deoxyoligonucleotides (Oligo645 and Oligo2142) followed by mung bean digestion. RP-HPLC analysis with these fragments was then carried out on a Supelcosil LC-18-S HPLC column (25 cm × 4.6 mm, 5 μm) equipped with a pre-column (4.6 × 20 mm) at 30°C on an Agilent 1200 HPLC system. The following amounts of digested RNA were loaded: (A) 1.9 μg, (B) 1.3 μg, (C) 2.9 μg and (D) 1.8 μg.

    Journal: Nucleic Acids Research

    Article Title: Yeast Rrp8p, a novel methyltransferase responsible for m1A 645 base modification of 25S rRNA

    doi: 10.1093/nar/gks1102

    Figure Lengend Snippet: RP-HPLC analysis of mung bean digested RNA fragments. Specific sequences of the 25S rRNA from wild-type ( A and C ) and the rrp8 -_ C mutant ( B and D ), corresponding to Helix 25.1 and Helix 65, respectively, were isolated by hybridization to complementary deoxyoligonucleotides (Oligo645 and Oligo2142) followed by mung bean digestion. RP-HPLC analysis with these fragments was then carried out on a Supelcosil LC-18-S HPLC column (25 cm × 4.6 mm, 5 μm) equipped with a pre-column (4.6 × 20 mm) at 30°C on an Agilent 1200 HPLC system. The following amounts of digested RNA were loaded: (A) 1.9 μg, (B) 1.3 μg, (C) 2.9 μg and (D) 1.8 μg.

    Article Snippet: Nucleosides were analysed by RP-HPLC on a Supelcosil LC-18-S HPLC column (25 cm × 4.6 mm, 5 µm) equipped with a pre-column (4.6 × 20 mm) at 30°C on an Agilent 1200 HPLC system.

    Techniques: High Performance Liquid Chromatography, Mutagenesis, Isolation, Hybridization

    Loss of Rrp8 influences the amount of 25S rRNA m1A modification. After sucrose gradient centrifugation, 60S subunits were collected with the Density Gradient Fractionation System (Teledyne Isco), and 25S rRNA was isolated. The 25S rRNA was digested with nuclease P1 and bacterial alkaline phosphatase (Sigma-Aldrich). Nucleosides from the wild-type ( A ) and the rrp8 -_ C mutant ( B ) were analysed by RP-HPLC on a Supelcosil LC-18-S HPLC column (25 cm × 4.6 mm, 5 μm) equipped with a pre-column (4.6 × 20 mm) at 30°C on an Agilent 1200 HPLC system. ( C ) Localization of m 1 A modifications of 25S rRNA is shown in the secondary structure of Helix 25.1 and Helix 65 ( http://www.rna.icmb.utexas.edu/ ). ( D ) 3D structure of the corresponding helices was made using PyMol software (PyMOL Molecular Graphics System, Version 1.2r3pre, Schröinger, LLC) using the recent 80S ribosome structure (3U5D.pdb and 3U5E.pdb). RNA is coloured in green, whereas the modified bases are shown in red spheres.

    Journal: Nucleic Acids Research

    Article Title: Yeast Rrp8p, a novel methyltransferase responsible for m1A 645 base modification of 25S rRNA

    doi: 10.1093/nar/gks1102

    Figure Lengend Snippet: Loss of Rrp8 influences the amount of 25S rRNA m1A modification. After sucrose gradient centrifugation, 60S subunits were collected with the Density Gradient Fractionation System (Teledyne Isco), and 25S rRNA was isolated. The 25S rRNA was digested with nuclease P1 and bacterial alkaline phosphatase (Sigma-Aldrich). Nucleosides from the wild-type ( A ) and the rrp8 -_ C mutant ( B ) were analysed by RP-HPLC on a Supelcosil LC-18-S HPLC column (25 cm × 4.6 mm, 5 μm) equipped with a pre-column (4.6 × 20 mm) at 30°C on an Agilent 1200 HPLC system. ( C ) Localization of m 1 A modifications of 25S rRNA is shown in the secondary structure of Helix 25.1 and Helix 65 ( http://www.rna.icmb.utexas.edu/ ). ( D ) 3D structure of the corresponding helices was made using PyMol software (PyMOL Molecular Graphics System, Version 1.2r3pre, Schröinger, LLC) using the recent 80S ribosome structure (3U5D.pdb and 3U5E.pdb). RNA is coloured in green, whereas the modified bases are shown in red spheres.

    Article Snippet: Nucleosides were analysed by RP-HPLC on a Supelcosil LC-18-S HPLC column (25 cm × 4.6 mm, 5 µm) equipped with a pre-column (4.6 × 20 mm) at 30°C on an Agilent 1200 HPLC system.

    Techniques: Modification, Gradient Centrifugation, Fractionation, Isolation, Mutagenesis, High Performance Liquid Chromatography, Software

    SDR9C7 catalyzes NAD + -dependent oxidation of 13-hydroxy-linoleate derivatives. ( A ). Middle panel: SDR9C7 catalyzes oxidation of the epoxy-alcohol 9 R ,10 R - trans -epoxy-11 E -13 R -hydroxy-octadecenoate methyl ester ( RRR -EpOH-Me) to the 13-ketone. Lower panel: the SDR9C7 R276C mutant has no detectable activity in oxidation of RRR -EpOH-Me, (as further confirmed by HPLC analysis of the incubation). ( B ) Reversed-phase HPLC analysis of the SDR9C7-catalyzed oxidation of RRR -EpOH-Me. The unreacted substrate is detected in the channel monitoring 205 nm, the single product mainly at 235 nm. ( C ) The 9,10-epoxy-11 E -13-keto product was identified from its cochromatography with the authentic standard and by its characteristic UV spectrum. The HPLC analysis used an Agilent 1200 series system with an Agilent Eclipse XBD-C18 column (5 μm, 15 × 0.46 cm), a solvent of acetonitrile/water/glacial acetic acid (75/25/0.01 by volume) at a flow rate of 1 mL/min, with the diode array detector set to monitor at 205, 220, 235, and 270 nm.

    Journal: The Journal of Clinical Investigation

    Article Title: SDR9C7 catalyzes critical dehydrogenation of acylceramides for skin barrier formation

    doi: 10.1172/JCI130675

    Figure Lengend Snippet: SDR9C7 catalyzes NAD + -dependent oxidation of 13-hydroxy-linoleate derivatives. ( A ). Middle panel: SDR9C7 catalyzes oxidation of the epoxy-alcohol 9 R ,10 R - trans -epoxy-11 E -13 R -hydroxy-octadecenoate methyl ester ( RRR -EpOH-Me) to the 13-ketone. Lower panel: the SDR9C7 R276C mutant has no detectable activity in oxidation of RRR -EpOH-Me, (as further confirmed by HPLC analysis of the incubation). ( B ) Reversed-phase HPLC analysis of the SDR9C7-catalyzed oxidation of RRR -EpOH-Me. The unreacted substrate is detected in the channel monitoring 205 nm, the single product mainly at 235 nm. ( C ) The 9,10-epoxy-11 E -13-keto product was identified from its cochromatography with the authentic standard and by its characteristic UV spectrum. The HPLC analysis used an Agilent 1200 series system with an Agilent Eclipse XBD-C18 column (5 μm, 15 × 0.46 cm), a solvent of acetonitrile/water/glacial acetic acid (75/25/0.01 by volume) at a flow rate of 1 mL/min, with the diode array detector set to monitor at 205, 220, 235, and 270 nm.

    Article Snippet: Initial screening of the products was conducted on an Agilent 1200 series HPLC system with the diode array detector set to monitor 205, 220, 235, and 270 nm.

    Techniques: Mutagenesis, Activity Assay, High Performance Liquid Chromatography, Incubation

    Effect of hypercholesterolemia on striatal dopamine level in Parkinsonian mice. Mice were sacrificed by decapitation on the seventh day following the first dose of MPTP. Striatal dopamine content was analyzed by HPLC-ECD system. Hypercholesterolemia exaggerates striatal dopamine depletion in Parkinsonian mice. The results are given as mean ± S.E.M. *p ≤ 0.05 as compared to control (CS) and #p ≤ 0.05 as compared to MPTP alone treated group (n = 6).

    Journal: PLoS ONE

    Article Title: Cholesterol contributes to dopamine-neuronal loss in MPTP mouse model of Parkinson’s disease: Involvement of mitochondrial dysfunctions and oxidative stress

    doi: 10.1371/journal.pone.0171285

    Figure Lengend Snippet: Effect of hypercholesterolemia on striatal dopamine level in Parkinsonian mice. Mice were sacrificed by decapitation on the seventh day following the first dose of MPTP. Striatal dopamine content was analyzed by HPLC-ECD system. Hypercholesterolemia exaggerates striatal dopamine depletion in Parkinsonian mice. The results are given as mean ± S.E.M. *p ≤ 0.05 as compared to control (CS) and #p ≤ 0.05 as compared to MPTP alone treated group (n = 6).

    Article Snippet: After sonication in ice-cold 0.1 M HClO4 , containing 0.01% EDTA, the tissues were centrifuged for 5 min at 10,000 x g 10 μL supernatant was injected into the HPLC system equipped with the Electro-Chemical detector (HPLC-ECD; Waters, Austria) at a flow rate 0.8 ml/min.

    Techniques: Mouse Assay, High Performance Liquid Chromatography

    Effect of hypercholesterolemia on nigrostriatal reduced glutathione (GSH) level in Parkinsonian mice. (A) Striatum and (B) substantia nigra regions of brain were used for estimating GSH levels by employing a sensitive HPLC-ECD system. Data are expressed as nmol/mg tissue and represented as mean ± S.E.M. *p ≤ 0.05 as compared with control and #p ≤ 0.05 as compared with MPTP alone treated group (n = 5).

    Journal: PLoS ONE

    Article Title: Cholesterol contributes to dopamine-neuronal loss in MPTP mouse model of Parkinson’s disease: Involvement of mitochondrial dysfunctions and oxidative stress

    doi: 10.1371/journal.pone.0171285

    Figure Lengend Snippet: Effect of hypercholesterolemia on nigrostriatal reduced glutathione (GSH) level in Parkinsonian mice. (A) Striatum and (B) substantia nigra regions of brain were used for estimating GSH levels by employing a sensitive HPLC-ECD system. Data are expressed as nmol/mg tissue and represented as mean ± S.E.M. *p ≤ 0.05 as compared with control and #p ≤ 0.05 as compared with MPTP alone treated group (n = 5).

    Article Snippet: After sonication in ice-cold 0.1 M HClO4 , containing 0.01% EDTA, the tissues were centrifuged for 5 min at 10,000 x g 10 μL supernatant was injected into the HPLC system equipped with the Electro-Chemical detector (HPLC-ECD; Waters, Austria) at a flow rate 0.8 ml/min.

    Techniques: Mouse Assay, High Performance Liquid Chromatography

    Effect of hypercholesterolemia on hydroxyl radical (•OH) generation in (A,C,E) striatum and (B,D,F) substantia nigra regions of brain of Parkinsonian mice. Animals were injected with salicylic acid (100 mg/kg) and sacrificed two hours post injection on the last day of treatment. 2,3- and 2,5-dihydroxy benzoic acid (DHBA; •OH adducts of salicylate) formed were measured from homogenates of NCP and SN by employing a sensitive HPLC-ECD method. Data are expressed as pmol/mg tissue and represented as mean ± S.E.M. *p ≤ 0.05 as compared with control and #p ≤ 0.05 as compared with MPTP alone treated group (n = 5).

    Journal: PLoS ONE

    Article Title: Cholesterol contributes to dopamine-neuronal loss in MPTP mouse model of Parkinson’s disease: Involvement of mitochondrial dysfunctions and oxidative stress

    doi: 10.1371/journal.pone.0171285

    Figure Lengend Snippet: Effect of hypercholesterolemia on hydroxyl radical (•OH) generation in (A,C,E) striatum and (B,D,F) substantia nigra regions of brain of Parkinsonian mice. Animals were injected with salicylic acid (100 mg/kg) and sacrificed two hours post injection on the last day of treatment. 2,3- and 2,5-dihydroxy benzoic acid (DHBA; •OH adducts of salicylate) formed were measured from homogenates of NCP and SN by employing a sensitive HPLC-ECD method. Data are expressed as pmol/mg tissue and represented as mean ± S.E.M. *p ≤ 0.05 as compared with control and #p ≤ 0.05 as compared with MPTP alone treated group (n = 5).

    Article Snippet: After sonication in ice-cold 0.1 M HClO4 , containing 0.01% EDTA, the tissues were centrifuged for 5 min at 10,000 x g 10 μL supernatant was injected into the HPLC system equipped with the Electro-Chemical detector (HPLC-ECD; Waters, Austria) at a flow rate 0.8 ml/min.

    Techniques: Mouse Assay, Injection, High Performance Liquid Chromatography

    A chromatogram of standard ginsenosides using HPLC assay. The column configuration consisted of an IMtakt Cadenza CD-C18 (4.6×75 mm). The UV absorption was measured at 203 nm. Gradient elution was employed, using solvent A (10% acetonitrile) and solvent B (90% acetonitrile) at 40℃. CK, compound K.

    Journal: Journal of Ginseng Research

    Article Title: The bioavailability of red ginseng extract fermented by Phellinus linteus

    doi: 10.5142/jgr.2013.37.108

    Figure Lengend Snippet: A chromatogram of standard ginsenosides using HPLC assay. The column configuration consisted of an IMtakt Cadenza CD-C18 (4.6×75 mm). The UV absorption was measured at 203 nm. Gradient elution was employed, using solvent A (10% acetonitrile) and solvent B (90% acetonitrile) at 40℃. CK, compound K.

    Article Snippet: HPLC analysis of ginsenosides A purified sample for HPLC analysis was prepared by C18 ODS cartridge (Waters Associates, Milford, MA, USA) solid-phase extraction according to a method described previously .

    Techniques: High Performance Liquid Chromatography

    A chromatogram of (A) non-fermented red ginseng and (B) fermented red ginseng by Phellinus linteus ginsenosides using HPLC assay. The column configuration consisted of an IMtakt Cadenza CD-C18 (4.6×75 mm). The UV absorption was measured at 203 nm. Gradient elution was employed, using solvent A (10% acetonitrile) and solvent B (90% acetonitrile) at 40℃.

    Journal: Journal of Ginseng Research

    Article Title: The bioavailability of red ginseng extract fermented by Phellinus linteus

    doi: 10.5142/jgr.2013.37.108

    Figure Lengend Snippet: A chromatogram of (A) non-fermented red ginseng and (B) fermented red ginseng by Phellinus linteus ginsenosides using HPLC assay. The column configuration consisted of an IMtakt Cadenza CD-C18 (4.6×75 mm). The UV absorption was measured at 203 nm. Gradient elution was employed, using solvent A (10% acetonitrile) and solvent B (90% acetonitrile) at 40℃.

    Article Snippet: HPLC analysis of ginsenosides A purified sample for HPLC analysis was prepared by C18 ODS cartridge (Waters Associates, Milford, MA, USA) solid-phase extraction according to a method described previously .

    Techniques: High Performance Liquid Chromatography

    HPLC chromatogram of glibenclamide in the presence of 30% H 2 O 2

    Journal: Iranian Journal of Pharmaceutical Research : IJPR

    Article Title: Rapid Analysis of Glibenclamide Using an Environmentally Benign Stability-Indicating RP-HPLC Method

    doi:

    Figure Lengend Snippet: HPLC chromatogram of glibenclamide in the presence of 30% H 2 O 2

    Article Snippet: Instrumentation and chromatographic conditions Liquid chromatographic identification of glibenclamide was performed at room temperature (25 ± 1 o C), with Waters HPLC system (Waters, USA).

    Techniques: High Performance Liquid Chromatography

    HPLC chromatogram of glibenclamide in methanol: ethanol (50:50 % v/v) with retention time of 2.551 min

    Journal: Iranian Journal of Pharmaceutical Research : IJPR

    Article Title: Rapid Analysis of Glibenclamide Using an Environmentally Benign Stability-Indicating RP-HPLC Method

    doi:

    Figure Lengend Snippet: HPLC chromatogram of glibenclamide in methanol: ethanol (50:50 % v/v) with retention time of 2.551 min

    Article Snippet: Instrumentation and chromatographic conditions Liquid chromatographic identification of glibenclamide was performed at room temperature (25 ± 1 o C), with Waters HPLC system (Waters, USA).

    Techniques: High Performance Liquid Chromatography

    HPLC chromatogram of glibenclamide in the presence of 0.1M HCl

    Journal: Iranian Journal of Pharmaceutical Research : IJPR

    Article Title: Rapid Analysis of Glibenclamide Using an Environmentally Benign Stability-Indicating RP-HPLC Method

    doi:

    Figure Lengend Snippet: HPLC chromatogram of glibenclamide in the presence of 0.1M HCl

    Article Snippet: Instrumentation and chromatographic conditions Liquid chromatographic identification of glibenclamide was performed at room temperature (25 ± 1 o C), with Waters HPLC system (Waters, USA).

    Techniques: High Performance Liquid Chromatography

    HPLC chromatogram of glibenclamide in the presence of 0.1M NaOH

    Journal: Iranian Journal of Pharmaceutical Research : IJPR

    Article Title: Rapid Analysis of Glibenclamide Using an Environmentally Benign Stability-Indicating RP-HPLC Method

    doi:

    Figure Lengend Snippet: HPLC chromatogram of glibenclamide in the presence of 0.1M NaOH

    Article Snippet: Instrumentation and chromatographic conditions Liquid chromatographic identification of glibenclamide was performed at room temperature (25 ± 1 o C), with Waters HPLC system (Waters, USA).

    Techniques: High Performance Liquid Chromatography

    HPLC chromatogram of glibenclamide under thermal condition

    Journal: Iranian Journal of Pharmaceutical Research : IJPR

    Article Title: Rapid Analysis of Glibenclamide Using an Environmentally Benign Stability-Indicating RP-HPLC Method

    doi:

    Figure Lengend Snippet: HPLC chromatogram of glibenclamide under thermal condition

    Article Snippet: Instrumentation and chromatographic conditions Liquid chromatographic identification of glibenclamide was performed at room temperature (25 ± 1 o C), with Waters HPLC system (Waters, USA).

    Techniques: High Performance Liquid Chromatography

    Figure 1. RP-HPLC chromatogram of ( A ) Cell culture harvest and ( B ) mAb1 Protein A intermediate.

    Journal: mAbs

    Article Title: Characterization of antibody variants during process development

    doi: 10.4161/mabs.21614

    Figure Lengend Snippet: Figure 1. RP-HPLC chromatogram of ( A ) Cell culture harvest and ( B ) mAb1 Protein A intermediate.

    Article Snippet: RP-HPLC of mAb1 was performed on a Waters nanoAcquity UPLC system consisting of a temperature-controlled autosampler.

    Techniques: High Performance Liquid Chromatography, Cell Culture

    Figure 6. LC/ESI-MS of the leader peptide. ( A ) The molecular mass of the peptide is detected at 3262.8153 Da. ( B ) LC/ESI-MS/MS of the leader peptide ( m/z 1088.26, 3+) of mAb1 enriched in RP-HPLC post peak.

    Journal: mAbs

    Article Title: Characterization of antibody variants during process development

    doi: 10.4161/mabs.21614

    Figure Lengend Snippet: Figure 6. LC/ESI-MS of the leader peptide. ( A ) The molecular mass of the peptide is detected at 3262.8153 Da. ( B ) LC/ESI-MS/MS of the leader peptide ( m/z 1088.26, 3+) of mAb1 enriched in RP-HPLC post peak.

    Article Snippet: RP-HPLC of mAb1 was performed on a Waters nanoAcquity UPLC system consisting of a temperature-controlled autosampler.

    Techniques: Mass Spectrometry, High Performance Liquid Chromatography

    Figure 5. LC/ESI-MS/MS in DDA mode of trypsin-digested and PNGase F-deglycosylated mAb1 enriched in RP-HPLC post peak. The leader peptide (2–31 HC) eluted at 127.04 min in the TIC.

    Journal: mAbs

    Article Title: Characterization of antibody variants during process development

    doi: 10.4161/mabs.21614

    Figure Lengend Snippet: Figure 5. LC/ESI-MS/MS in DDA mode of trypsin-digested and PNGase F-deglycosylated mAb1 enriched in RP-HPLC post peak. The leader peptide (2–31 HC) eluted at 127.04 min in the TIC.

    Article Snippet: RP-HPLC of mAb1 was performed on a Waters nanoAcquity UPLC system consisting of a temperature-controlled autosampler.

    Techniques: Mass Spectrometry, High Performance Liquid Chromatography

    Figure 4. LC/ESI-MS of DTT treated heavy chains of mAb1 ( A ) control and ( B ) enriched in RP-HPLC post peak.

    Journal: mAbs

    Article Title: Characterization of antibody variants during process development

    doi: 10.4161/mabs.21614

    Figure Lengend Snippet: Figure 4. LC/ESI-MS of DTT treated heavy chains of mAb1 ( A ) control and ( B ) enriched in RP-HPLC post peak.

    Article Snippet: RP-HPLC of mAb1 was performed on a Waters nanoAcquity UPLC system consisting of a temperature-controlled autosampler.

    Techniques: Mass Spectrometry, High Performance Liquid Chromatography

    Figure 2. Overlays of ( A ) RP-HPLC; ( B ) SEC-HPLC; and ( C ) IEX-HPLC chromatograms of mAb1 control and mAb1 enriched in RP-HPLC post peak.

    Journal: mAbs

    Article Title: Characterization of antibody variants during process development

    doi: 10.4161/mabs.21614

    Figure Lengend Snippet: Figure 2. Overlays of ( A ) RP-HPLC; ( B ) SEC-HPLC; and ( C ) IEX-HPLC chromatograms of mAb1 control and mAb1 enriched in RP-HPLC post peak.

    Article Snippet: RP-HPLC of mAb1 was performed on a Waters nanoAcquity UPLC system consisting of a temperature-controlled autosampler.

    Techniques: High Performance Liquid Chromatography, Size-exclusion Chromatography

    Figure 3. LC/ESI-MS of PNGase F deglycosylated mAb1 ( A ) control and ( B ) enriched in RP-HPLC post peak.

    Journal: mAbs

    Article Title: Characterization of antibody variants during process development

    doi: 10.4161/mabs.21614

    Figure Lengend Snippet: Figure 3. LC/ESI-MS of PNGase F deglycosylated mAb1 ( A ) control and ( B ) enriched in RP-HPLC post peak.

    Article Snippet: RP-HPLC of mAb1 was performed on a Waters nanoAcquity UPLC system consisting of a temperature-controlled autosampler.

    Techniques: Mass Spectrometry, High Performance Liquid Chromatography

    RP-HPLC post peak is due to the presence of unprocessed secretion leader on the N-terminus of mAb1 heavy chain

    Journal: mAbs

    Article Title: Characterization of antibody variants during process development

    doi: 10.4161/mabs.21614

    Figure Lengend Snippet: RP-HPLC post peak is due to the presence of unprocessed secretion leader on the N-terminus of mAb1 heavy chain

    Article Snippet: RP-HPLC of mAb1 was performed on a Waters nanoAcquity UPLC system consisting of a temperature-controlled autosampler.

    Techniques: High Performance Liquid Chromatography

    ( a ) Reverse phase high performance liquid chromatography (HPLC) chromatogram of skin secretion of Phyllomedusa camba monitored at 214 nm. The arrow indicated the retention time of PSN-PC; ( b ) Tandem mass (MS/MS) fragmentation spectrum of PSN-PC; ( c ) Predicted singly-charged b ions and y ions arising from MS/MS fragmentation. The observed b- and y-ions were indicated in blue and red typefaces.

    Journal: Molecules : A Journal of Synthetic Chemistry and Natural Product Chemistry

    Article Title: PSN-PC: A Novel Antimicrobial and Anti-Biofilm Peptide from the Skin Secretion of Phyllomedusa-camba with Cytotoxicity on Human Lung Cancer Cell

    doi: 10.3390/molecules22111896

    Figure Lengend Snippet: ( a ) Reverse phase high performance liquid chromatography (HPLC) chromatogram of skin secretion of Phyllomedusa camba monitored at 214 nm. The arrow indicated the retention time of PSN-PC; ( b ) Tandem mass (MS/MS) fragmentation spectrum of PSN-PC; ( c ) Predicted singly-charged b ions and y ions arising from MS/MS fragmentation. The observed b- and y-ions were indicated in blue and red typefaces.

    Article Snippet: The authenticity of the purified synthetic PSN-PC was verified by RP-HPLC with an analytical Jupiter C5 column (250 mm × 4.6 mm, Phenomenex, UK).

    Techniques: High Performance Liquid Chromatography, Mass Spectrometry

    ( a ) The RP-HPLC chromatogram of the purified synthetic phylloseptin-PC (PSN-PC); ( b ) MALDI-TOF mass spectrum of synthetic PSN-PC; ( c ) Predicted secondary structure of PSN-PC using I-TASSER; ( d ) Predicted 3D model of PSN-PC using I-TASSER; ( e ) Z-score plot using ProSA-web; ( f ) Helical wheel plot of PSN-PC; ( g ) Circular dichroism (CD) spectra recorded for PSN-PC (100 μM) in 10 mM ammonium acetate buffer and 50% TFE ammonium acetate buffer.

    Journal: Molecules : A Journal of Synthetic Chemistry and Natural Product Chemistry

    Article Title: PSN-PC: A Novel Antimicrobial and Anti-Biofilm Peptide from the Skin Secretion of Phyllomedusa-camba with Cytotoxicity on Human Lung Cancer Cell

    doi: 10.3390/molecules22111896

    Figure Lengend Snippet: ( a ) The RP-HPLC chromatogram of the purified synthetic phylloseptin-PC (PSN-PC); ( b ) MALDI-TOF mass spectrum of synthetic PSN-PC; ( c ) Predicted secondary structure of PSN-PC using I-TASSER; ( d ) Predicted 3D model of PSN-PC using I-TASSER; ( e ) Z-score plot using ProSA-web; ( f ) Helical wheel plot of PSN-PC; ( g ) Circular dichroism (CD) spectra recorded for PSN-PC (100 μM) in 10 mM ammonium acetate buffer and 50% TFE ammonium acetate buffer.

    Article Snippet: The authenticity of the purified synthetic PSN-PC was verified by RP-HPLC with an analytical Jupiter C5 column (250 mm × 4.6 mm, Phenomenex, UK).

    Techniques: High Performance Liquid Chromatography, Purification

    Solid-phase purification of the phosphorothioate DNA sequence 10b . RP-HPLC analysis of solid-phase-purified 12b that was released from the support 11b . Inset: Purity analysis of the solid-phase-purified 12b by PAGE. Abbreviation: BP, bromophenol blue dye.

    Journal: Current protocols in nucleic acid chemistry

    Article Title: A High-Throughput Process for the Solid-Phase Purification of Synthetic DNA Sequences

    doi: 10.1002/cpnc.31

    Figure Lengend Snippet: Solid-phase purification of the phosphorothioate DNA sequence 10b . RP-HPLC analysis of solid-phase-purified 12b that was released from the support 11b . Inset: Purity analysis of the solid-phase-purified 12b by PAGE. Abbreviation: BP, bromophenol blue dye.

    Article Snippet: The purity of these sequences has been evaluated by RP-HPLC and by PAGE under denaturing conditions ( , , , and ).

    Techniques: Purification, Sequencing, High Performance Liquid Chromatography, Polyacrylamide Gel Electrophoresis

    Solid-phase purification of the native DNA sequence 10f . RP-HPLC analysis of solid-phase-purified 12f that was released from the support 11f . Inset: Purity analysis of the solid-phase-purified 12f by PAGE. Abbreviation: BP, bromophenol blue dye.

    Journal: Current protocols in nucleic acid chemistry

    Article Title: A High-Throughput Process for the Solid-Phase Purification of Synthetic DNA Sequences

    doi: 10.1002/cpnc.31

    Figure Lengend Snippet: Solid-phase purification of the native DNA sequence 10f . RP-HPLC analysis of solid-phase-purified 12f that was released from the support 11f . Inset: Purity analysis of the solid-phase-purified 12f by PAGE. Abbreviation: BP, bromophenol blue dye.

    Article Snippet: The purity of these sequences has been evaluated by RP-HPLC and by PAGE under denaturing conditions ( , , , and ).

    Techniques: Purification, Sequencing, High Performance Liquid Chromatography, Polyacrylamide Gel Electrophoresis

    Solid-phase purification of the phosphorothioate DNA sequence 10a . RP-HPLC analysis of solid-phase-purified 12a that was released from the support 11a . Inset: Purity analysis of the solid-phase-purified 12a by PAGE. Chromatographic conditions are reported in the annotation of step 3 of Basic Protocol 4 . Abbreviation: BP, bromophenol blue dye.

    Journal: Current protocols in nucleic acid chemistry

    Article Title: A High-Throughput Process for the Solid-Phase Purification of Synthetic DNA Sequences

    doi: 10.1002/cpnc.31

    Figure Lengend Snippet: Solid-phase purification of the phosphorothioate DNA sequence 10a . RP-HPLC analysis of solid-phase-purified 12a that was released from the support 11a . Inset: Purity analysis of the solid-phase-purified 12a by PAGE. Chromatographic conditions are reported in the annotation of step 3 of Basic Protocol 4 . Abbreviation: BP, bromophenol blue dye.

    Article Snippet: The purity of these sequences has been evaluated by RP-HPLC and by PAGE under denaturing conditions ( , , , and ).

    Techniques: Purification, Sequencing, High Performance Liquid Chromatography, Polyacrylamide Gel Electrophoresis

    Solid-phase purification of the phosphorothioate DNA sequence 10c . RP-HPLC analysis of solid-phase-purified 12c that was released from the support 11c . Inset: Purity analysis of the solid-phase-purified 12c by PAGE. Abbreviation: BP, bromophenol blue dye.

    Journal: Current protocols in nucleic acid chemistry

    Article Title: A High-Throughput Process for the Solid-Phase Purification of Synthetic DNA Sequences

    doi: 10.1002/cpnc.31

    Figure Lengend Snippet: Solid-phase purification of the phosphorothioate DNA sequence 10c . RP-HPLC analysis of solid-phase-purified 12c that was released from the support 11c . Inset: Purity analysis of the solid-phase-purified 12c by PAGE. Abbreviation: BP, bromophenol blue dye.

    Article Snippet: The purity of these sequences has been evaluated by RP-HPLC and by PAGE under denaturing conditions ( , , , and ).

    Techniques: Purification, Sequencing, High Performance Liquid Chromatography, Polyacrylamide Gel Electrophoresis

    10-Fold scale up solid-phase purification of the phosphorothioate DNA sequence 12a. (A) RP-HPLC profile of unpurified 10a . (B) RP-HPLC profile of unpurified 10a after capture by the support 3 . (C) RP-HPLC analysis of solid-phase purified 12a that has been released from the support 11a . (D) Photograph of precipitated 12a accounting for 995 OD 260 of the DNA sequence. Inset: Purity analysis of the solid-phase purified 12a by PAGE. Abbreviation: BP, bromophenol blue dye.

    Journal: Current protocols in nucleic acid chemistry

    Article Title: A High-Throughput Process for the Solid-Phase Purification of Synthetic DNA Sequences

    doi: 10.1002/cpnc.31

    Figure Lengend Snippet: 10-Fold scale up solid-phase purification of the phosphorothioate DNA sequence 12a. (A) RP-HPLC profile of unpurified 10a . (B) RP-HPLC profile of unpurified 10a after capture by the support 3 . (C) RP-HPLC analysis of solid-phase purified 12a that has been released from the support 11a . (D) Photograph of precipitated 12a accounting for 995 OD 260 of the DNA sequence. Inset: Purity analysis of the solid-phase purified 12a by PAGE. Abbreviation: BP, bromophenol blue dye.

    Article Snippet: The purity of these sequences has been evaluated by RP-HPLC and by PAGE under denaturing conditions ( , , , and ).

    Techniques: Purification, Sequencing, High Performance Liquid Chromatography, Polyacrylamide Gel Electrophoresis

    Solid-phase purification of the phosphorothioate DNA sequence 10d . RP-HPLC analysis of solid-phase-purified 12d that was released from the support 11d . Inset: Purity analysis of the solid-phase-purified 12d by PAGE. Abbreviation: BP, bromophenol blue dye.

    Journal: Current protocols in nucleic acid chemistry

    Article Title: A High-Throughput Process for the Solid-Phase Purification of Synthetic DNA Sequences

    doi: 10.1002/cpnc.31

    Figure Lengend Snippet: Solid-phase purification of the phosphorothioate DNA sequence 10d . RP-HPLC analysis of solid-phase-purified 12d that was released from the support 11d . Inset: Purity analysis of the solid-phase-purified 12d by PAGE. Abbreviation: BP, bromophenol blue dye.

    Article Snippet: The purity of these sequences has been evaluated by RP-HPLC and by PAGE under denaturing conditions ( , , , and ).

    Techniques: Purification, Sequencing, High Performance Liquid Chromatography, Polyacrylamide Gel Electrophoresis