reversed phase hplc  (Thermo Fisher)


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    Structured Review

    Thermo Fisher reversed phase hplc
    In vitro Glutathione conjugation of <t>2MB2</t> in presence of challengers. Glutathione conjugation of 2MB2 was determined by <t>HPLC</t> measurement, after incubation during 80 min at 37 °C of 2MB2 + reduced glutathione in presence of OE homogenate from newborn rabbits. 2MB2 enzymatic glutathione conjugation was compared to those obtained in presence of a challenger compound at equimolar concentration (ratio 1:1, A ) and 3 times more concentrated (ratio 1:3, B ). Results are expressed as % of the glutathione-2MB2 conjugate amount; 100% being obtained for 2MB2 alone. The % are means of n = 3–5 replicated measures ± SEM. *, ** and *** indicate significant differences (p ≤ 0.05, p ≤ 0.01 and p ≤ 0.001 respectively) between the control (2MB2 alone) and mixture conditions (Kruskal-Wallis multiple comparisons followed by a Conover-Iman post-hoc test). Odorant abbreviations: 2MB2: 2-methylbut-2-enal (the mammary pheromone), 2MP2: 2-methylpent-2-enal, Cinnam: Cinnamaldehyde, EA: ethyl acetate.
    Reversed Phase Hplc, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 124 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/reversed phase hplc/product/Thermo Fisher
    Average 99 stars, based on 124 article reviews
    Price from $9.99 to $1999.99
    reversed phase hplc - by Bioz Stars, 2020-11
    99/100 stars

    Images

    1) Product Images from "Odorant-odorant metabolic interaction, a novel actor in olfactory perception and behavioral responsiveness"

    Article Title: Odorant-odorant metabolic interaction, a novel actor in olfactory perception and behavioral responsiveness

    Journal: Scientific Reports

    doi: 10.1038/s41598-017-10080-z

    In vitro Glutathione conjugation of 2MB2 in presence of challengers. Glutathione conjugation of 2MB2 was determined by HPLC measurement, after incubation during 80 min at 37 °C of 2MB2 + reduced glutathione in presence of OE homogenate from newborn rabbits. 2MB2 enzymatic glutathione conjugation was compared to those obtained in presence of a challenger compound at equimolar concentration (ratio 1:1, A ) and 3 times more concentrated (ratio 1:3, B ). Results are expressed as % of the glutathione-2MB2 conjugate amount; 100% being obtained for 2MB2 alone. The % are means of n = 3–5 replicated measures ± SEM. *, ** and *** indicate significant differences (p ≤ 0.05, p ≤ 0.01 and p ≤ 0.001 respectively) between the control (2MB2 alone) and mixture conditions (Kruskal-Wallis multiple comparisons followed by a Conover-Iman post-hoc test). Odorant abbreviations: 2MB2: 2-methylbut-2-enal (the mammary pheromone), 2MP2: 2-methylpent-2-enal, Cinnam: Cinnamaldehyde, EA: ethyl acetate.
    Figure Legend Snippet: In vitro Glutathione conjugation of 2MB2 in presence of challengers. Glutathione conjugation of 2MB2 was determined by HPLC measurement, after incubation during 80 min at 37 °C of 2MB2 + reduced glutathione in presence of OE homogenate from newborn rabbits. 2MB2 enzymatic glutathione conjugation was compared to those obtained in presence of a challenger compound at equimolar concentration (ratio 1:1, A ) and 3 times more concentrated (ratio 1:3, B ). Results are expressed as % of the glutathione-2MB2 conjugate amount; 100% being obtained for 2MB2 alone. The % are means of n = 3–5 replicated measures ± SEM. *, ** and *** indicate significant differences (p ≤ 0.05, p ≤ 0.01 and p ≤ 0.001 respectively) between the control (2MB2 alone) and mixture conditions (Kruskal-Wallis multiple comparisons followed by a Conover-Iman post-hoc test). Odorant abbreviations: 2MB2: 2-methylbut-2-enal (the mammary pheromone), 2MP2: 2-methylpent-2-enal, Cinnam: Cinnamaldehyde, EA: ethyl acetate.

    Techniques Used: In Vitro, Conjugation Assay, High Performance Liquid Chromatography, Incubation, Concentration Assay

    2) Product Images from "Purification of Bioactive Lipopeptides Produced by Bacillus subtilis Strain BIA"

    Article Title: Purification of Bioactive Lipopeptides Produced by Bacillus subtilis Strain BIA

    Journal: Chromatographia

    doi: 10.1007/s10337-016-3164-3

    Purification of lipopeptides by reversed-phase HPLC on a Thermo Hypersil-Keystone ODS column. A segmented gradient was used and product eluted at 75 % of acetonitrile. Flow rate was maintained at 1 mL/min
    Figure Legend Snippet: Purification of lipopeptides by reversed-phase HPLC on a Thermo Hypersil-Keystone ODS column. A segmented gradient was used and product eluted at 75 % of acetonitrile. Flow rate was maintained at 1 mL/min

    Techniques Used: Purification, High Performance Liquid Chromatography, Flow Cytometry

    3) Product Images from "The Human Cathelicidin Antimicrobial Peptide LL-37 Promotes the Growth of the Pulmonary Pathogen Aspergillus fumigatus"

    Article Title: The Human Cathelicidin Antimicrobial Peptide LL-37 Promotes the Growth of the Pulmonary Pathogen Aspergillus fumigatus

    Journal: Infection and Immunity

    doi: 10.1128/IAI.00097-18

    Gliotoxin quantification in A. fumigatus supernatants exposed to LL-37 (5 μg/ml), scrambled LL-37 (5 μg/ml), or DMSO (0.5% [vol/vol]) for 24 or 48 h was determined by RP-HPLC. Exposure to LL-37 increased gliotoxin levels at 24 and 48 h (*, P
    Figure Legend Snippet: Gliotoxin quantification in A. fumigatus supernatants exposed to LL-37 (5 μg/ml), scrambled LL-37 (5 μg/ml), or DMSO (0.5% [vol/vol]) for 24 or 48 h was determined by RP-HPLC. Exposure to LL-37 increased gliotoxin levels at 24 and 48 h (*, P

    Techniques Used: High Performance Liquid Chromatography

    Related Articles

    Reversed-phase Chromatography:

    Article Title: Proteomics Profiling of KAIMRC1 in Comparison to MDA-MB231 and MCF-7
    Article Snippet: .. High pH Reverse-Phase Peptide Fractionation Each TMT pooled labeled sample was fractionated offline on the basis of high pH (basic) reversed-phase chromatography prior to LC-MS/MS. .. Following the manufacture instruction, peptide sample was fractionated into 8 fractions using Pierce™ High pH Reversed-Phase Peptide Fractionation Kit (Thermo).

    Article Title: Proteomic Profile of Mouse Brain Aging Contributions to Mitochondrial Dysfunction, DNA Oxidative Damage, Loss of Neurotrophic Factor, and Synaptic and Ribosomal Proteins
    Article Snippet: .. High-pH Reversed-Phase Chromatography Separation Labeled peptides were fractionated by Pierce High-pH Reversed-Phase Peptide Fractionation Kit (Thermo Fisher 84868) for further NanoLC-ESI-MS/MS analysis. .. First, the adjustment of the spin columns consisted of removing the solution, packing the resin material, and washing the spin column twice with 300 μ L acetonitrile (ACN) and 0.1% FA solution, respectively, all of which were centrifuged at 5,000 × g for 2 min. Second, peptide separation involved dissolving each sample with 300 μ L of 0.1% FA, loading onto a column, and eluting twice with a gradient elution solution of 300 μ L (ACN: triethylamine) (Thermo Fisher 84868 (5%, 10%, 12.5%, 15%, 17.5%, 20.0%, 22.5%, 25.0%, and 50.0%)), all of which were maintained at 3,000 × g for 2 min. After drying in a vacuum concentrator, 20 μL of 0.1% FA was added to each tube for NanoLC-ESI-MS/MS analysis.

    Centrifugation:

    Article Title: Synaptotagmin 17 controls neurite outgrowth and synaptic physiology via distinct cellular pathways
    Article Snippet: .. TMT-labeled samples were combined at a 1:1:1:1:1:1:1:1 ratio, vacuum-centrifuged to near dryness, subjected to High pH Reversed-Phase Peptide Fractionation (Pierce), followed by C18 extraction (Pierce), and vacuum centrifugation to dryness. .. Three micrograms of each sample was auto-sampler loaded with a Thermo RSLC UPLC pump onto a vented Acclaim Pepmap 100, 75 µm × 2 cm, nanoViper trap column coupled to a nanoViper analytical column (cat. #: 164570, Thermo, 3 µm, 100 Å, C18, 0.075 mm, 500 mm) with stainless steel emitter tip assembled on the Nanospray Flex Ion Source with a spray voltage of 2000 V. A coupled Orbitrap Fusion (Thermo Fisher Scientific) was used to generate MS data.

    Fractionation:

    Article Title: Screening of differentially expressed proteins from syncytiotrophoblast for severe early-onset preeclampsia in women with gestational diabetes mellitus using tandem mass tag quantitative proteomics
    Article Snippet: .. After TMT labelling, the digested sample was fractionated into 10 fractions, and the excess label and salts were removed, according to Pierce High pH Reversed-Phase Fractionation Kit Manual (Thermo Fisher Scientific). .. Liquid chromatography–mass spectrometry/mass spectrometry analysis Each fraction, dissolved into solution A (0.1% formic acid), was loaded into a reverse phase trap column (Thermo Scientific Acclaim PepMap100, 100 μm × 2 cm, nanoViper C18) connected to the C18-reversed phase analytical column (Thermo Scientific Easy Column, 10 cm long, 75-μm inner diameter, 3-μm resin) and separated with a linear gradient of solution B (84% acetonitrile and 0.1% formic acid) at a flow rate of 300 nL/min.

    Article Title: Flow-cytometric microglial sorting coupled with quantitative proteomics identifies moesin as a highly-abundant microglial protein with relevance to Alzheimer’s disease
    Article Snippet: .. High pH reversed-phase peptide fractionation High pH reversed-phase peptide fractionation kit was used to perform desalting and fractionation as per manufacturer’s protocol (ThermoFisher, Cat. No. 84868). .. Briefly, the dried sample containing all ten TMT channels was reconstituted with 300µL of 0.1% TFA and added to conditioned reversed-phase fractionation spin columns containing 20mg of resin in a 1:1 water/DMSO slurry.

    Article Title: Proteomic signatures of acute oxidative stress response to paraquat in the mouse heart
    Article Snippet: .. Samples were then subjected to offline reversed phase fractionation (8 fractions) using a Pierce High-pH Reversed Phase Fractionation Kit (Thermo Fisher) according to the manufacturer’s instructions for fractionation of TMT-labeled samples. .. Liquid chromatography-tandem mass spectrometry was performed on fractionated labeled peptides.

    Labeling:

    Article Title: Proteomics Profiling of KAIMRC1 in Comparison to MDA-MB231 and MCF-7
    Article Snippet: .. High pH Reverse-Phase Peptide Fractionation Each TMT pooled labeled sample was fractionated offline on the basis of high pH (basic) reversed-phase chromatography prior to LC-MS/MS. .. Following the manufacture instruction, peptide sample was fractionated into 8 fractions using Pierce™ High pH Reversed-Phase Peptide Fractionation Kit (Thermo).

    Article Title: Proteomic Profile of Mouse Brain Aging Contributions to Mitochondrial Dysfunction, DNA Oxidative Damage, Loss of Neurotrophic Factor, and Synaptic and Ribosomal Proteins
    Article Snippet: .. High-pH Reversed-Phase Chromatography Separation Labeled peptides were fractionated by Pierce High-pH Reversed-Phase Peptide Fractionation Kit (Thermo Fisher 84868) for further NanoLC-ESI-MS/MS analysis. .. First, the adjustment of the spin columns consisted of removing the solution, packing the resin material, and washing the spin column twice with 300 μ L acetonitrile (ACN) and 0.1% FA solution, respectively, all of which were centrifuged at 5,000 × g for 2 min. Second, peptide separation involved dissolving each sample with 300 μ L of 0.1% FA, loading onto a column, and eluting twice with a gradient elution solution of 300 μ L (ACN: triethylamine) (Thermo Fisher 84868 (5%, 10%, 12.5%, 15%, 17.5%, 20.0%, 22.5%, 25.0%, and 50.0%)), all of which were maintained at 3,000 × g for 2 min. After drying in a vacuum concentrator, 20 μL of 0.1% FA was added to each tube for NanoLC-ESI-MS/MS analysis.

    Peptide Fractionation:

    Article Title: Flow-cytometric microglial sorting coupled with quantitative proteomics identifies moesin as a highly-abundant microglial protein with relevance to Alzheimer’s disease
    Article Snippet: .. High pH reversed-phase peptide fractionation High pH reversed-phase peptide fractionation kit was used to perform desalting and fractionation as per manufacturer’s protocol (ThermoFisher, Cat. No. 84868). .. Briefly, the dried sample containing all ten TMT channels was reconstituted with 300µL of 0.1% TFA and added to conditioned reversed-phase fractionation spin columns containing 20mg of resin in a 1:1 water/DMSO slurry.

    Article Title: Proteomics Profiling of KAIMRC1 in Comparison to MDA-MB231 and MCF-7
    Article Snippet: .. High pH Reverse-Phase Peptide Fractionation Each TMT pooled labeled sample was fractionated offline on the basis of high pH (basic) reversed-phase chromatography prior to LC-MS/MS. .. Following the manufacture instruction, peptide sample was fractionated into 8 fractions using Pierce™ High pH Reversed-Phase Peptide Fractionation Kit (Thermo).

    Article Title: Synaptotagmin 17 controls neurite outgrowth and synaptic physiology via distinct cellular pathways
    Article Snippet: .. TMT-labeled samples were combined at a 1:1:1:1:1:1:1:1 ratio, vacuum-centrifuged to near dryness, subjected to High pH Reversed-Phase Peptide Fractionation (Pierce), followed by C18 extraction (Pierce), and vacuum centrifugation to dryness. .. Three micrograms of each sample was auto-sampler loaded with a Thermo RSLC UPLC pump onto a vented Acclaim Pepmap 100, 75 µm × 2 cm, nanoViper trap column coupled to a nanoViper analytical column (cat. #: 164570, Thermo, 3 µm, 100 Å, C18, 0.075 mm, 500 mm) with stainless steel emitter tip assembled on the Nanospray Flex Ion Source with a spray voltage of 2000 V. A coupled Orbitrap Fusion (Thermo Fisher Scientific) was used to generate MS data.

    Article Title: Proteomics Profiling of KAIMRC1 in Comparison to MDA-MB231 and MCF-7
    Article Snippet: .. Following the manufacture instruction, peptide sample was fractionated into 8 fractions using Pierce™ High pH Reversed-Phase Peptide Fractionation Kit (Thermo). ..

    Article Title: Secretome profiling of PC3/nKR cells, a novel highly migrating prostate cancer subline derived from PC3 cells
    Article Snippet: .. The peptide mixture was fractionated using a high-pH reverse-phase peptide fractionation kit (Thermo Fisher Scientific) according to the manufacturer’s procedure. .. Totally, 8 fractionated peptides were cleaned using ZipTip pipette tips (Millipore) to remove the salt and completely dried by a speed vacuum system followed by liquid chromatography-tandem mass spectrometry (LC-MS/MS).

    Article Title: Proteomic Profile of Mouse Brain Aging Contributions to Mitochondrial Dysfunction, DNA Oxidative Damage, Loss of Neurotrophic Factor, and Synaptic and Ribosomal Proteins
    Article Snippet: .. High-pH Reversed-Phase Chromatography Separation Labeled peptides were fractionated by Pierce High-pH Reversed-Phase Peptide Fractionation Kit (Thermo Fisher 84868) for further NanoLC-ESI-MS/MS analysis. .. First, the adjustment of the spin columns consisted of removing the solution, packing the resin material, and washing the spin column twice with 300 μ L acetonitrile (ACN) and 0.1% FA solution, respectively, all of which were centrifuged at 5,000 × g for 2 min. Second, peptide separation involved dissolving each sample with 300 μ L of 0.1% FA, loading onto a column, and eluting twice with a gradient elution solution of 300 μ L (ACN: triethylamine) (Thermo Fisher 84868 (5%, 10%, 12.5%, 15%, 17.5%, 20.0%, 22.5%, 25.0%, and 50.0%)), all of which were maintained at 3,000 × g for 2 min. After drying in a vacuum concentrator, 20 μL of 0.1% FA was added to each tube for NanoLC-ESI-MS/MS analysis.

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    Thermo Fisher betasil c18 rp hplc column
    <t>HPLC-MS</t> analysis of cowpea extracts for destruxin (DTX) production. (A) Analysis of not colonized (free of fungus) plants (negative control); (B) plants endophytically colonized by Metarhizium robertsii ARSEF 2575; and (C) not-colonized plants spiked with DTX standards (positive control). The cowpea seeds, both fungus-inoculated and control (not colonized) were incubated on moist filter paper under optimal light (16L∶8D) and temperature (25°C) conditions for 12 days at which time the germlings had developed roots, stems, cotyledons and two true leaves. DTXs were extracted from entire plants using methanol 100% and <t>SPE-C18</t> cartridges.
    Betasil C18 Rp Hplc Column, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/betasil c18 rp hplc column/product/Thermo Fisher
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    betasil c18 rp hplc column - by Bioz Stars, 2020-11
    99/100 stars
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    94
    Thermo Fisher rp hplc
    Identification and purification of disulphide-bonded peptides from a tryptic digest of Pf332 DBL domain. A. Comparison of the analytical <t>RP-HPLC</t> elution profiles for DTT-reduced and non-reduced tryptic digest of refolded Pf332 DBL domain. Reduced (upper trace) and non-reduced (lower trace) digests (20 μg) were fractionated on a Vydac <t>C18</t> (4.6 mm inner diameter × 250 mm) column under identical chromatographic conditions. The column was developed at a flow rate of 1 ml min −1 with a linear 120 min gradient from 0 to 70% buffer B, where buffer A was 0.05% (v/v) trifluoroacetic acid in Milli Q water, and buffer B was 0.05% (v/v) trifluoroacetic acid in acetonitrile. Asterisk-labelled peaks within the non-reduced chromatogram represent those altered by DTT reduction. B. Preparative scale RP-HPLC purification of peptides from the tryptic digest of Pf332 DBL domain. A total of 125 μg of digest was fractionated by elution from a Vydac C18 column (4.6 mm inner diameter × 250 mm) column using the elution conditions described in (A). Peptide fractions found to contain disulphide-bonded peptides by Edman degradation and mass spectrometry are indicated by peak numbers and correspond to those given in Table 1 (see Experimental procedures for further details).
    Rp Hplc, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 133 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rp hplc/product/Thermo Fisher
    Average 94 stars, based on 133 article reviews
    Price from $9.99 to $1999.99
    rp hplc - by Bioz Stars, 2020-11
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    91
    Thermo Fisher high performance liquid chromatography hplc analysis reverse phase hplc
    <t>RP-HPLC</t> Analysis of Propolis from T. Sirindhornae (column: 250 mm X 4.6 mm, 5 μM,λ 250 nm). Standard compounds: caffeic acid (1), apigenin (2), p-coumaric acid (3), and pinocembrin (4) (A). Component analysis of <t>DMEP-A</t> (B), DMEP-B (C) and DMEP-C (D) are indicated by the black lines.
    High Performance Liquid Chromatography Hplc Analysis Reverse Phase Hplc, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/high performance liquid chromatography hplc analysis reverse phase hplc/product/Thermo Fisher
    Average 91 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    high performance liquid chromatography hplc analysis reverse phase hplc - by Bioz Stars, 2020-11
    91/100 stars
      Buy from Supplier

    Image Search Results


    HPLC-MS analysis of cowpea extracts for destruxin (DTX) production. (A) Analysis of not colonized (free of fungus) plants (negative control); (B) plants endophytically colonized by Metarhizium robertsii ARSEF 2575; and (C) not-colonized plants spiked with DTX standards (positive control). The cowpea seeds, both fungus-inoculated and control (not colonized) were incubated on moist filter paper under optimal light (16L∶8D) and temperature (25°C) conditions for 12 days at which time the germlings had developed roots, stems, cotyledons and two true leaves. DTXs were extracted from entire plants using methanol 100% and SPE-C18 cartridges.

    Journal: PLoS ONE

    Article Title: Production of Destruxins from Metarhizium spp. Fungi in Artificial Medium and in Endophytically Colonized Cowpea Plants

    doi: 10.1371/journal.pone.0104946

    Figure Lengend Snippet: HPLC-MS analysis of cowpea extracts for destruxin (DTX) production. (A) Analysis of not colonized (free of fungus) plants (negative control); (B) plants endophytically colonized by Metarhizium robertsii ARSEF 2575; and (C) not-colonized plants spiked with DTX standards (positive control). The cowpea seeds, both fungus-inoculated and control (not colonized) were incubated on moist filter paper under optimal light (16L∶8D) and temperature (25°C) conditions for 12 days at which time the germlings had developed roots, stems, cotyledons and two true leaves. DTXs were extracted from entire plants using methanol 100% and SPE-C18 cartridges.

    Article Snippet: The LC-MS system consisted of a Betasil C18 RP HPLC column (100×2.1 mm, Thermo Fisher), coupled to a Surveyor MS Pump Plus, a Surveyor Auto Sampler Plus and a PDA UV–vis absorbance detector in-line with an LCQ Advantage Max mass spectrometer and electrospray (esi) ionization source (Thermo Electron Corp, San Jose, CA, USA).

    Techniques: High Performance Liquid Chromatography, Mass Spectrometry, Negative Control, Positive Control, Incubation

    Identification and purification of disulphide-bonded peptides from a tryptic digest of Pf332 DBL domain. A. Comparison of the analytical RP-HPLC elution profiles for DTT-reduced and non-reduced tryptic digest of refolded Pf332 DBL domain. Reduced (upper trace) and non-reduced (lower trace) digests (20 μg) were fractionated on a Vydac C18 (4.6 mm inner diameter × 250 mm) column under identical chromatographic conditions. The column was developed at a flow rate of 1 ml min −1 with a linear 120 min gradient from 0 to 70% buffer B, where buffer A was 0.05% (v/v) trifluoroacetic acid in Milli Q water, and buffer B was 0.05% (v/v) trifluoroacetic acid in acetonitrile. Asterisk-labelled peaks within the non-reduced chromatogram represent those altered by DTT reduction. B. Preparative scale RP-HPLC purification of peptides from the tryptic digest of Pf332 DBL domain. A total of 125 μg of digest was fractionated by elution from a Vydac C18 column (4.6 mm inner diameter × 250 mm) column using the elution conditions described in (A). Peptide fractions found to contain disulphide-bonded peptides by Edman degradation and mass spectrometry are indicated by peak numbers and correspond to those given in Table 1 (see Experimental procedures for further details).

    Journal: Molecular Microbiology

    Article Title: Analysis of structure and function of the giant protein Pf332 in Plasmodium falciparum

    doi: 10.1111/j.1365-2958.2008.06508.x

    Figure Lengend Snippet: Identification and purification of disulphide-bonded peptides from a tryptic digest of Pf332 DBL domain. A. Comparison of the analytical RP-HPLC elution profiles for DTT-reduced and non-reduced tryptic digest of refolded Pf332 DBL domain. Reduced (upper trace) and non-reduced (lower trace) digests (20 μg) were fractionated on a Vydac C18 (4.6 mm inner diameter × 250 mm) column under identical chromatographic conditions. The column was developed at a flow rate of 1 ml min −1 with a linear 120 min gradient from 0 to 70% buffer B, where buffer A was 0.05% (v/v) trifluoroacetic acid in Milli Q water, and buffer B was 0.05% (v/v) trifluoroacetic acid in acetonitrile. Asterisk-labelled peaks within the non-reduced chromatogram represent those altered by DTT reduction. B. Preparative scale RP-HPLC purification of peptides from the tryptic digest of Pf332 DBL domain. A total of 125 μg of digest was fractionated by elution from a Vydac C18 column (4.6 mm inner diameter × 250 mm) column using the elution conditions described in (A). Peptide fractions found to contain disulphide-bonded peptides by Edman degradation and mass spectrometry are indicated by peak numbers and correspond to those given in Table 1 (see Experimental procedures for further details).

    Article Snippet: The subdigest of tryptic fraction #35 was analysed after clean-up on C18 ZipTip (Millipore, Bedford, MA, USA) by RP-HPLC on a C18 column (3 μm, 0.15 mm inner diameter × 150 mm, Vydac) using a Surveyor-MS HPLC system (Thermo, San Jose, CA, USA).

    Techniques: Purification, High Performance Liquid Chromatography, Flow Cytometry, Mass Spectrometry

    RP-HPLC Analysis of Propolis from T. Sirindhornae (column: 250 mm X 4.6 mm, 5 μM,λ 250 nm). Standard compounds: caffeic acid (1), apigenin (2), p-coumaric acid (3), and pinocembrin (4) (A). Component analysis of DMEP-A (B), DMEP-B (C) and DMEP-C (D) are indicated by the black lines.

    Journal: Asian Pacific Journal of Cancer Prevention : APJCP

    Article Title: Cytotoxic Activity of Propolis Extracts from the Stingless Bee Trigona Sirindhornae Against Primary and Metastatic Head and Neck Cancer Cell Lines

    doi: 10.22034/APJCP.2017.18.4.1051

    Figure Lengend Snippet: RP-HPLC Analysis of Propolis from T. Sirindhornae (column: 250 mm X 4.6 mm, 5 μM,λ 250 nm). Standard compounds: caffeic acid (1), apigenin (2), p-coumaric acid (3), and pinocembrin (4) (A). Component analysis of DMEP-A (B), DMEP-B (C) and DMEP-C (D) are indicated by the black lines.

    Article Snippet: High performance liquid chromatography (HPLC) analysis Reverse-phase HPLC (RP-HPLC) analysis of the DMEP fractions was performed using an HPLC Spectra system equipped with a P4000 pump and a quaternary gradient pump system, a UV6000LP diode-array detector, and an AS3000 autosampler (Thermo Separation Products, Fremont, CA).

    Techniques: High Performance Liquid Chromatography