rp-hplc Search Results


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  • 99
    Millipore rp hplc
    Rp Hplc, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 371 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 99 stars, based on 371 article reviews
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    94
    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 2110 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 94 stars, based on 2110 article reviews
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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 2100 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 94 stars, based on 2100 article reviews
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    93
    Shimadzu Corporation rp hplc
    Analytical <t>HPLC</t> of purified <t>mSAM.</t> Gradient of 50–100% acetonitrile. RT: 10.7 min (lower panel), 11.5 min (upper panel). Absorbances at 450 nm (coumarin 343), 540 nm (TAMRA), 254 nm, and 280 nm are shown. Both 5-(6-)TAMRA isomers are shown separately (upper and lower panel).
    Rp Hplc, supplied by Shimadzu Corporation, used in various techniques. Bioz Stars score: 93/100, based on 823 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Thermo Fisher rp hplc
    <t>RP-HPLC</t> of tryptic peptides from the CB12 pool comparing fetal and 3-month calf cartilages. The <t>C8</t> RP-HPLC elution profiles (0–30% gradient) of the isolated CB12 pools are shown ( A ). Tandem mass spectra compare ketoimine ( B ) and adduct ( C ) versions
    Rp Hplc, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 973 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Waters Corporation preparative rp hplc
    Purification of stingray ghrelin-like peptide (GRLN-LP) from stomach extracts . Black bars indicate the measured fluorescence changes in intracellular calcium ion concentrations in CHO cells expressing rat GHS-R1a (CHO-GHSR62). (A) Carboxymethyl (CM)-cation ion-exchange <t>HPLC</t> (pH 4.8) of the SP-III fraction of stomach extracts. The GRLN-like activity was divided into four groups (A-D). (B) Preparative reverse-phase (RP)-HPLC (Symmetry <t>C18,</t> 3.9 × 150 mm) of group B after purification with an anti-rat GRLN1-11 immuno-affinity column. (C) Final purification of the active fraction indicated in (B) by another RP-HPLC (Vydac diphenyl, 219TP5215, 2.1 × 150 mm).
    Preparative Rp Hplc, supplied by Waters Corporation, used in various techniques. Bioz Stars score: 92/100, based on 315 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Hitachi Ltd rp hplc
    <t>RP-HPLC</t> separation of TPIs from N. attenuata of the wild-type genotype. Numbers refer to <t>TPI</t> fractions containing inhibitory activity against trypsin. RP-HPLC profile of TPIs from uninduced control leaves (dashed line, right y axis) and leaves elicited
    Rp Hplc, supplied by Hitachi Ltd, used in various techniques. Bioz Stars score: 93/100, based on 261 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    JASCO Inc reversed phase hplc
    Association of hemolymph HemaP with the fat body after feeding diet. A , preparation of iodinated HemaP; <t>RP-HPLC</t> profile of <t>rHemaP</t> ( upper panel ) and iodinated HemaP ( lower panel ). The identity of iodinated rHemaP (indicated by the arrow ), which eluted faster than rHemaP, was confirmed by MALDI-TOF MS analyses (data not shown). The main product was confirmed to be di-iodinated rHemaP (I-rHemaP). *, a peak corresponding to unreacted rHemaP. X , a peak derived from excess reagents. B , bioassay of I-rHemaP. I-rHemaP induced foraging activity at levels similar to rHemaP (5 μg) compared with vehicle injection. **, p
    Reversed Phase Hplc, supplied by JASCO Inc, used in various techniques. Bioz Stars score: 91/100, based on 41 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 91 stars, based on 41 article reviews
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    91
    Phenomenex preparative reversed phase hplc
    Association of hemolymph HemaP with the fat body after feeding diet. A , preparation of iodinated HemaP; <t>RP-HPLC</t> profile of <t>rHemaP</t> ( upper panel ) and iodinated HemaP ( lower panel ). The identity of iodinated rHemaP (indicated by the arrow ), which eluted faster than rHemaP, was confirmed by MALDI-TOF MS analyses (data not shown). The main product was confirmed to be di-iodinated rHemaP (I-rHemaP). *, a peak corresponding to unreacted rHemaP. X , a peak derived from excess reagents. B , bioassay of I-rHemaP. I-rHemaP induced foraging activity at levels similar to rHemaP (5 μg) compared with vehicle injection. **, p
    Preparative Reversed Phase Hplc, supplied by Phenomenex, used in various techniques. Bioz Stars score: 91/100, based on 121 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Merck & Co reversed phase hplc
    Translocation. A. Colicin E3-cleaved (closed circles) or control (open circles) pre-translocation complexes (0.1 μM) were mixed in a quench-flow apparatus with EF-G·GTP (3 μM) and Pmn (10 mM) and translocation analysed by formation of <t>fMetPhe-Pmn.</t> The amount of pre-translocation complex (PTC) was determined by <t>HPLC</t> analysis of fMetPhe. B. Translocation was monitored by the fluorescence change of fMetPhe-tRNA Phe (Prf16/17). Curve 1 – control ribosomes; curve 2 – colicin E3-cleaved ribosomes; curve 3 – control ribosomes in the presence of viomycin (200 μM); curve 4 – colicin E3-cleaved ribosomes with viomycin (200 μM). Normalized ΔF, fluorescence change normalized by the maximum extent of translocation determined by the Pmn reaction. C. Pi release upon GTP hydrolysis by EF-G (curves 1 and 2) or buffer control (curves 3 and 4) with control ribosomes (curves 1 and 3) or colicin E3-cleaved (curves 2 and 4). Pi release was measured by the fluorescence change of MDCC-PBP upon Pi binding ( Experimental procedures ). D. Multiple-turnover GTP hydrolysis by EF-G. Velocity of GTP hydrolysis was measured with catalytic concentrations of EF-G (10 nM) and increasing concentrations of colicin E3-cleaved ribosomes (closed circles) or control ribosomes (open circles) in the presence of excess [γ- 32 P]-GTP (200 μM).
    Reversed Phase Hplc, supplied by Merck & Co, used in various techniques. Bioz Stars score: 94/100, based on 220 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Phenomenex rp hplc column
    Distinct HRNR-derived CIDAMPs show similar ribosomal protein binding patterns. ( a ) SulfoLink®–column-bound proteins of an E . coli -extract were separated on a Jupiter® <t>C18</t> <t>RP-HPLC</t> column with a Prp-gradient. HPLC fractions containing UV-absorbing peaks (C1–D10) were divided into five aliquots and adjusted in parallel to five PAGE-gels and separated. ( b ) Silver-stained proteins. ( c ) HRNR-Far-Western blot for probing with biotinylated HR1-18 (HRNR 2556–2677 ) using Strep - Tactin ®, ( d ) HRNR-Far-Western blot for probing with biotinylated rSumo3-HRNR 2591–2684 using Strep - Tactin ®, ( e ) HRNR-Far-Western blot for probing with rHRNR 2591–2684 using anti-HRNR 2591–2684 antibodies, ( f ) HRNR-Far-Western blot for probing with rHRNR 1075–1172 using anti-HRNR 1075–1172 antibodies. Note similarities of the staining patterns, irrespective the CIDAMP AA-sequence or biotin-labeling and irrespective whether a Strep - Tactin ®- or antibody-detectable CIDAMP was used to probe and detect the target protein on the membrane. Note the presence of 70 kDa bands upon HRNR-Far-Western blot analyses in most of the investigated HPLC fractions with highest intensity for rHRNR 1075–1172 binding ( f ). The most intensive band, corresponding to a 37 kDa protein in fraction number C13, was identified as E . coli ribosomal protein L2.
    Rp Hplc Column, supplied by Phenomenex, used in various techniques. Bioz Stars score: 91/100, based on 95 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Phenomenex semi preparative rp hplc
    Recombinant production of <t>Mb1a.</t> Semi-preparative <t>RP-HPLC</t> chromatogram of recombinant Mb1a released by TEV protease cleavage of the MBP-Mb1a fusion protein (see Materials and Methods for more details). The dotted line indicates the gradient of solvent B (90% acetonitrile/0.043% TFA). Top inset: SDS-PAGE gel showing pre-cleaved MBP-Mb1a fusion protein (lane 1) and remaining MBP after cleavage (lane 2). Lane M contains molecular markers (masses in kDa). Bottom inset: MALDI-TOF mass spectrum of pure recombinant Mb1a.
    Semi Preparative Rp Hplc, supplied by Phenomenex, used in various techniques. Bioz Stars score: 90/100, based on 89 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Gilson Inc rp hplc
    Recombinant production of <t>Mb1a.</t> Semi-preparative <t>RP-HPLC</t> chromatogram of recombinant Mb1a released by TEV protease cleavage of the MBP-Mb1a fusion protein (see Materials and Methods for more details). The dotted line indicates the gradient of solvent B (90% acetonitrile/0.043% TFA). Top inset: SDS-PAGE gel showing pre-cleaved MBP-Mb1a fusion protein (lane 1) and remaining MBP after cleavage (lane 2). Lane M contains molecular markers (masses in kDa). Bottom inset: MALDI-TOF mass spectrum of pure recombinant Mb1a.
    Rp Hplc, supplied by Gilson Inc, used in various techniques. Bioz Stars score: 93/100, based on 207 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Supelco reversed phase hplc
    Isolation of vurtoxin and Vur-S49 by reverse-phase <t>HPLC.</t> Separation was done on a Discovery <t>BIO</t> Wide Pore C18 column (10×250 mm, Supelco) in a gradient of 25–40% (v/v) acetonitrile in 60 min in the presence of 0.1% (v/v) trifluoroacetic acid, at a flow rate of 2.0 ml/min. Fraction containing Vur-S49 (4) and vurtoxin (11) are indicated by horizontal bars.
    Reversed Phase Hplc, supplied by Supelco, used in various techniques. Bioz Stars score: 92/100, based on 136 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Agilent technologies reversed phase high performance liquid chromatography rp hplc
    Effect of DB3 and DB3DB3 on different <t>Aβ</t> aggregation species. A) Analysis of Aβ(1–42) aggregation species with density gradient centrifugation and followed by analysis using silver-stained Tricine-SDS-PAGE to analyze the influence of DB3 and DB3DB3 on the distribution of Aβ assemblies. B) Quantification of Aβ(1–42) by <t>RP-HPLC.</t> All data were recorded in triplicate.
    Reversed Phase High Performance Liquid Chromatography Rp Hplc, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 93/100, based on 385 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    MACHEREY NAGEL rp hplc
    LOX-mediated oxidation of PU-NAEs. Oxidation of PU-NAEs relative to PU-FFA by heterologously expressed AtLOX1–6 , to their corresponding hydroperoxides (and chemical reduction to hydroxides), is shown in A . The products <t>NAE-HOD</t> and NAE-HOT were further separated on <t>NP-HPLC</t> to identify the preferred position of oxygenation ( B and C , respectively). Error bars show the standard deviation of three independent experiments.
    Rp Hplc, supplied by MACHEREY NAGEL, used in various techniques. Bioz Stars score: 92/100, based on 165 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Hewlett-Packard rp hplc
    <t>HPLC</t> profiles on a C-18 analytical column of 1 as reference (top) and of aliquots withdrawn from incubation of the <t>nucleopeptide</t> in 94% fresh human serum at 37 °C at different times (detection at 260 nm).
    Rp Hplc, supplied by Hewlett-Packard, used in various techniques. Bioz Stars score: 92/100, based on 105 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Agilent technologies preparative rp hplc
    <t>HPLC</t> profiles on a C-18 analytical column of 1 as reference (top) and of aliquots withdrawn from incubation of the <t>nucleopeptide</t> in 94% fresh human serum at 37 °C at different times (detection at 260 nm).
    Preparative Rp Hplc, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 92/100, based on 169 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Waters Corporation semi preparative rp hplc
    <t>HPLC</t> profiles on a C-18 analytical column of 1 as reference (top) and of aliquots withdrawn from incubation of the <t>nucleopeptide</t> in 94% fresh human serum at 37 °C at different times (detection at 260 nm).
    Semi Preparative Rp Hplc, supplied by Waters Corporation, used in various techniques. Bioz Stars score: 90/100, based on 113 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Shimadzu Corporation preparative rp hplc
    <t>HPLC</t> profiles on a C-18 analytical column of 1 as reference (top) and of aliquots withdrawn from incubation of the <t>nucleopeptide</t> in 94% fresh human serum at 37 °C at different times (detection at 260 nm).
    Preparative Rp Hplc, supplied by Shimadzu Corporation, used in various techniques. Bioz Stars score: 92/100, based on 179 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    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

    Purification of active fraction F2 using reverse phase high performance liquid chromatography (RP-HPLC) and the activities of sub-fractions assay: ( A ) percentage inhibition of hydrophilic and hydrophobic extracts of F2; ( B ) chromatogram of active fraction F2 by RP-HPLC, measured at 280 nm; ( C ) percentage inhibition of F2-1 and F2-2; and (D) H 2 O 2 production capacity of F2-1 and F2-2. Spots in ( A , C , D ) represent the raw data. The results are expressed as the mean ± standard deviation ( n = 3). The symbol of “**” and “*” in ( A , C , D ) represent significant differences of p

    Journal: Marine Drugs

    Article Title: Novel Antibacterial Peptides Isolated from the Maillard Reaction Products of Half-Fin Anchovy (Setipinna taty) Hydrolysates/Glucose and Their Mode of Action in Escherichia Coli

    doi: 10.3390/md17010047

    Figure Lengend Snippet: Purification of active fraction F2 using reverse phase high performance liquid chromatography (RP-HPLC) and the activities of sub-fractions assay: ( A ) percentage inhibition of hydrophilic and hydrophobic extracts of F2; ( B ) chromatogram of active fraction F2 by RP-HPLC, measured at 280 nm; ( C ) percentage inhibition of F2-1 and F2-2; and (D) H 2 O 2 production capacity of F2-1 and F2-2. Spots in ( A , C , D ) represent the raw data. The results are expressed as the mean ± standard deviation ( n = 3). The symbol of “**” and “*” in ( A , C , D ) represent significant differences of p

    Article Snippet: The hydrophobic extract of F2, which showed the largest percentage inhibition, was loaded onto a RP-HPLC system equipped with a C18 column (4.6 × 250 mm, 5 μm, Sunfire™, Waters, MA, USA) for further separation.

    Techniques: Purification, High Performance Liquid Chromatography, Inhibition, Standard Deviation

    ( 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

    Size exclusion and reversed-phase HPLC analysis of purified R0.6C. a Size exclusion chromatography was performed under native conditions in a phosphate buffer pH 6.7, to determine the amount of monomer in the sample. The peak corresponding to the monomer is indicated with the integrated area of the peak written above. b Reversed-phase HPLC–UV chromatograms recorded following analysis of purified protein batches. The peak at 17 min corresponds to monomeric R0.6C antigen

    Journal: Microbial Cell Factories

    Article Title: Construct design, production, and characterization of Plasmodium falciparum 48/45 R0.6C subunit protein produced in Lactococcus lactis as candidate vaccine

    doi: 10.1186/s12934-017-0710-0

    Figure Lengend Snippet: Size exclusion and reversed-phase HPLC analysis of purified R0.6C. a Size exclusion chromatography was performed under native conditions in a phosphate buffer pH 6.7, to determine the amount of monomer in the sample. The peak corresponding to the monomer is indicated with the integrated area of the peak written above. b Reversed-phase HPLC–UV chromatograms recorded following analysis of purified protein batches. The peak at 17 min corresponds to monomeric R0.6C antigen

    Article Snippet: SEC–HPLC and RP-HPLC analysis of R0.6C Native size exclusion high-performance liquid chromatography (SEC–HPLC) or reversed-phase HPLC (RP-HPLC) of intact R0.6C were performed using an Agilent 1100 Series HPLC System (Agilent Technologies, USA) equipped with a TSKgel G3000SWXL SEC column, 5 µm, 7.8 × 300 mm (Tosoh Bioscience, Japan) or equipped with a Vydac 214TP C4 reversed-phase column, 5 µm, 4.6 × 250 mm (The Separations Group, CA, US), respectively.

    Techniques: High Performance Liquid Chromatography, Purification, Size-exclusion Chromatography

    Analytical HPLC of purified mSAM. Gradient of 50–100% acetonitrile. RT: 10.7 min (lower panel), 11.5 min (upper panel). Absorbances at 450 nm (coumarin 343), 540 nm (TAMRA), 254 nm, and 280 nm are shown. Both 5-(6-)TAMRA isomers are shown separately (upper and lower panel).

    Journal: ACS Central Science

    Article Title: Cathepsin G Activity as a New Marker for Detecting Airway Inflammation by Microscopy and Flow Cytometry

    doi: 10.1021/acscentsci.8b00933

    Figure Lengend Snippet: Analytical HPLC of purified mSAM. Gradient of 50–100% acetonitrile. RT: 10.7 min (lower panel), 11.5 min (upper panel). Absorbances at 450 nm (coumarin 343), 540 nm (TAMRA), 254 nm, and 280 nm are shown. Both 5-(6-)TAMRA isomers are shown separately (upper and lower panel).

    Article Snippet: Reporter Purification sSAM and mSAM were analyzed and purified by RP-HPLC on a Shimadzu system equipped with a photodiode array detector (Duisburg, Germany).

    Techniques: High Performance Liquid Chromatography, Purification

    Mass spectra of sSAM. Expected masses: [M+1] + , 1902; [M+2] 2+ , 951; [M+3] 3+ , 634. The two spectra correspond to the two isomer peaks observed by HPLC ( Figure 6 ).

    Journal: ACS Central Science

    Article Title: Cathepsin G Activity as a New Marker for Detecting Airway Inflammation by Microscopy and Flow Cytometry

    doi: 10.1021/acscentsci.8b00933

    Figure Lengend Snippet: Mass spectra of sSAM. Expected masses: [M+1] + , 1902; [M+2] 2+ , 951; [M+3] 3+ , 634. The two spectra correspond to the two isomer peaks observed by HPLC ( Figure 6 ).

    Article Snippet: Reporter Purification sSAM and mSAM were analyzed and purified by RP-HPLC on a Shimadzu system equipped with a photodiode array detector (Duisburg, Germany).

    Techniques: High Performance Liquid Chromatography

    Analytical HPLC of purified sSAM. Gradient of 10–100% acetonitrile, RT: 9 and 9.5 min. Absorbance at 450 nm (coumarin 343), 540 nm (TAMRA), 254 nm, and 280 nm are shown. The two peaks represent the two 5-(6-)TAMRA isomers.

    Journal: ACS Central Science

    Article Title: Cathepsin G Activity as a New Marker for Detecting Airway Inflammation by Microscopy and Flow Cytometry

    doi: 10.1021/acscentsci.8b00933

    Figure Lengend Snippet: Analytical HPLC of purified sSAM. Gradient of 10–100% acetonitrile, RT: 9 and 9.5 min. Absorbance at 450 nm (coumarin 343), 540 nm (TAMRA), 254 nm, and 280 nm are shown. The two peaks represent the two 5-(6-)TAMRA isomers.

    Article Snippet: Reporter Purification sSAM and mSAM were analyzed and purified by RP-HPLC on a Shimadzu system equipped with a photodiode array detector (Duisburg, Germany).

    Techniques: High Performance Liquid Chromatography, Purification

    RP-HPLC of tryptic peptides from the CB12 pool comparing fetal and 3-month calf cartilages. The C8 RP-HPLC elution profiles (0–30% gradient) of the isolated CB12 pools are shown ( A ). Tandem mass spectra compare ketoimine ( B ) and adduct ( C ) versions

    Journal: The Journal of Biological Chemistry

    Article Title: Maturation of Collagen Ketoimine Cross-links by an Alternative Mechanism to Pyridinoline Formation in Cartilage *

    doi: 10.1074/jbc.M110.111534

    Figure Lengend Snippet: RP-HPLC of tryptic peptides from the CB12 pool comparing fetal and 3-month calf cartilages. The C8 RP-HPLC elution profiles (0–30% gradient) of the isolated CB12 pools are shown ( A ). Tandem mass spectra compare ketoimine ( B ) and adduct ( C ) versions

    Article Snippet: Each tryptic peptide pool from the IMAC column was run on RP-HPLC (C8 RP-300, 25 cm × 4.6 mm, Brownlee columns, Applied Biosystems) ( ).

    Techniques: High Performance Liquid Chromatography, Isolation

    Reverse-phase HPLC of Cu 2+ IMAC affinity column-resolved tryptic peptide pools from bovine type II collagen. Equivalent aliquots of each of the three peptide pools were eluted from a C8 column with a 0–40% gradient of acetonitrile: n -propanol (3:1

    Journal: The Journal of Biological Chemistry

    Article Title: Maturation of Collagen Ketoimine Cross-links by an Alternative Mechanism to Pyridinoline Formation in Cartilage *

    doi: 10.1074/jbc.M110.111534

    Figure Lengend Snippet: Reverse-phase HPLC of Cu 2+ IMAC affinity column-resolved tryptic peptide pools from bovine type II collagen. Equivalent aliquots of each of the three peptide pools were eluted from a C8 column with a 0–40% gradient of acetonitrile: n -propanol (3:1

    Article Snippet: Each tryptic peptide pool from the IMAC column was run on RP-HPLC (C8 RP-300, 25 cm × 4.6 mm, Brownlee columns, Applied Biosystems) ( ).

    Techniques: High Performance Liquid Chromatography, Affinity Column

    Purification of stingray ghrelin-like peptide (GRLN-LP) from stomach extracts . Black bars indicate the measured fluorescence changes in intracellular calcium ion concentrations in CHO cells expressing rat GHS-R1a (CHO-GHSR62). (A) Carboxymethyl (CM)-cation ion-exchange HPLC (pH 4.8) of the SP-III fraction of stomach extracts. The GRLN-like activity was divided into four groups (A-D). (B) Preparative reverse-phase (RP)-HPLC (Symmetry C18, 3.9 × 150 mm) of group B after purification with an anti-rat GRLN1-11 immuno-affinity column. (C) Final purification of the active fraction indicated in (B) by another RP-HPLC (Vydac diphenyl, 219TP5215, 2.1 × 150 mm).

    Journal: BMC Biochemistry

    Article Title: Ghrelin-like peptide with fatty acid modification and O-glycosylation in the red stingray, Dasyatis akajei

    doi: 10.1186/1471-2091-10-30

    Figure Lengend Snippet: Purification of stingray ghrelin-like peptide (GRLN-LP) from stomach extracts . Black bars indicate the measured fluorescence changes in intracellular calcium ion concentrations in CHO cells expressing rat GHS-R1a (CHO-GHSR62). (A) Carboxymethyl (CM)-cation ion-exchange HPLC (pH 4.8) of the SP-III fraction of stomach extracts. The GRLN-like activity was divided into four groups (A-D). (B) Preparative reverse-phase (RP)-HPLC (Symmetry C18, 3.9 × 150 mm) of group B after purification with an anti-rat GRLN1-11 immuno-affinity column. (C) Final purification of the active fraction indicated in (B) by another RP-HPLC (Vydac diphenyl, 219TP5215, 2.1 × 150 mm).

    Article Snippet: The samples were first applied to a preparative RP-HPLC with a Symmetry C18 column (3.9 × 150 mm, Waters) at a flow rate of 1 ml/min under a linear gradient from 10% to 60% acetonitlile containing 0.1% TFA for 40 min.

    Techniques: Purification, Fluorescence, Expressing, High Performance Liquid Chromatography, Activity Assay, Affinity Column

    RP-HPLC separation of TPIs from N. attenuata of the wild-type genotype. Numbers refer to TPI fractions containing inhibitory activity against trypsin. RP-HPLC profile of TPIs from uninduced control leaves (dashed line, right y axis) and leaves elicited

    Journal: Plant Physiology

    Article Title: Differential Elicitation of Two Processing Proteases Controls the Processing Pattern of the Trypsin Proteinase Inhibitor Precursor in Nicotiana attenuata 1

    doi: 10.1104/pp.105.064006

    Figure Lengend Snippet: RP-HPLC separation of TPIs from N. attenuata of the wild-type genotype. Numbers refer to TPI fractions containing inhibitory activity against trypsin. RP-HPLC profile of TPIs from uninduced control leaves (dashed line, right y axis) and leaves elicited

    Article Snippet: The total TPI pool was chromatographed on RP-HPLC performed on a Hitachi LaChrom L7100.

    Techniques: High Performance Liquid Chromatography, Activity Assay

    Chain composition of the two-chain TPI from N. attenuata . A, Separation of the chains. The purified two-chain TPI (5 μ g) was reductively carboxymethylated, and the liberated chains were purified by RP-HPLC (solid line). The position of the original

    Journal: Plant Physiology

    Article Title: Differential Elicitation of Two Processing Proteases Controls the Processing Pattern of the Trypsin Proteinase Inhibitor Precursor in Nicotiana attenuata 1

    doi: 10.1104/pp.105.064006

    Figure Lengend Snippet: Chain composition of the two-chain TPI from N. attenuata . A, Separation of the chains. The purified two-chain TPI (5 μ g) was reductively carboxymethylated, and the liberated chains were purified by RP-HPLC (solid line). The position of the original

    Article Snippet: The total TPI pool was chromatographed on RP-HPLC performed on a Hitachi LaChrom L7100.

    Techniques: Purification, High Performance Liquid Chromatography

    RP-HPLC separation of TPIs from the Arizona genotype S++, which was transformed with the TPI gene from Utah under control of a constitutive promoter to restore TPI production. Numbers refer to TPI fractions containing inhibitory activity

    Journal: Plant Physiology

    Article Title: Differential Elicitation of Two Processing Proteases Controls the Processing Pattern of the Trypsin Proteinase Inhibitor Precursor in Nicotiana attenuata 1

    doi: 10.1104/pp.105.064006

    Figure Lengend Snippet: RP-HPLC separation of TPIs from the Arizona genotype S++, which was transformed with the TPI gene from Utah under control of a constitutive promoter to restore TPI production. Numbers refer to TPI fractions containing inhibitory activity

    Article Snippet: The total TPI pool was chromatographed on RP-HPLC performed on a Hitachi LaChrom L7100.

    Techniques: High Performance Liquid Chromatography, Transformation Assay, Activity Assay

    Association of hemolymph HemaP with the fat body after feeding diet. A , preparation of iodinated HemaP; RP-HPLC profile of rHemaP ( upper panel ) and iodinated HemaP ( lower panel ). The identity of iodinated rHemaP (indicated by the arrow ), which eluted faster than rHemaP, was confirmed by MALDI-TOF MS analyses (data not shown). The main product was confirmed to be di-iodinated rHemaP (I-rHemaP). *, a peak corresponding to unreacted rHemaP. X , a peak derived from excess reagents. B , bioassay of I-rHemaP. I-rHemaP induced foraging activity at levels similar to rHemaP (5 μg) compared with vehicle injection. **, p

    Journal: The Journal of Biological Chemistry

    Article Title: Identification of a Novel Hemolymph Peptide That Modulates Silkworm Feeding Motivation *

    doi: 10.1074/jbc.M110.176016

    Figure Lengend Snippet: Association of hemolymph HemaP with the fat body after feeding diet. A , preparation of iodinated HemaP; RP-HPLC profile of rHemaP ( upper panel ) and iodinated HemaP ( lower panel ). The identity of iodinated rHemaP (indicated by the arrow ), which eluted faster than rHemaP, was confirmed by MALDI-TOF MS analyses (data not shown). The main product was confirmed to be di-iodinated rHemaP (I-rHemaP). *, a peak corresponding to unreacted rHemaP. X , a peak derived from excess reagents. B , bioassay of I-rHemaP. I-rHemaP induced foraging activity at levels similar to rHemaP (5 μg) compared with vehicle injection. **, p

    Article Snippet: The resulting iodinated rHemaP was purified using reversed-phase HPLC (Jasco SC-802, PU-980, UV-970) and eluted using the same linear gradient program as used in the final HemaP purification step.

    Techniques: High Performance Liquid Chromatography, Mass Spectrometry, Derivative Assay, Activity Assay, Injection

    Preparation of recombinant HemaP (rHemaP). A , purified rHemaP and larval hemolymph were subjected to SDS-PAGE and the resulting gel stained with Coomassie Brilliant Blue ( CBB ). B , MALDI-TOF MS analysis of the purified rHemaP. The isolated rHemaP was analyzed using MALDI-TOF MS. C , comparison of the RP-HPLC profile of B. mori ). D , biological activity of the fraction containing HemaP (fraction 22 as indicated in C ) separated from hemolymph with RP-HPLC. Vehicle and rHemaP (5 μg) were used as negative and positive controls, respectively. Biological activity was confirmed using a 10-μl hemolymph equivalent. The sample from fraction 22 was lyophilized to dry the mobile phase of RP-HPLC. No influence of the trace amount of TFA on the biological activity was confirmed. **, p

    Journal: The Journal of Biological Chemistry

    Article Title: Identification of a Novel Hemolymph Peptide That Modulates Silkworm Feeding Motivation *

    doi: 10.1074/jbc.M110.176016

    Figure Lengend Snippet: Preparation of recombinant HemaP (rHemaP). A , purified rHemaP and larval hemolymph were subjected to SDS-PAGE and the resulting gel stained with Coomassie Brilliant Blue ( CBB ). B , MALDI-TOF MS analysis of the purified rHemaP. The isolated rHemaP was analyzed using MALDI-TOF MS. C , comparison of the RP-HPLC profile of B. mori ). D , biological activity of the fraction containing HemaP (fraction 22 as indicated in C ) separated from hemolymph with RP-HPLC. Vehicle and rHemaP (5 μg) were used as negative and positive controls, respectively. Biological activity was confirmed using a 10-μl hemolymph equivalent. The sample from fraction 22 was lyophilized to dry the mobile phase of RP-HPLC. No influence of the trace amount of TFA on the biological activity was confirmed. **, p

    Article Snippet: The resulting iodinated rHemaP was purified using reversed-phase HPLC (Jasco SC-802, PU-980, UV-970) and eluted using the same linear gradient program as used in the final HemaP purification step.

    Techniques: Recombinant, Purification, SDS Page, Staining, Mass Spectrometry, Isolation, High Performance Liquid Chromatography, Activity Assay

    Translocation. A. Colicin E3-cleaved (closed circles) or control (open circles) pre-translocation complexes (0.1 μM) were mixed in a quench-flow apparatus with EF-G·GTP (3 μM) and Pmn (10 mM) and translocation analysed by formation of fMetPhe-Pmn. The amount of pre-translocation complex (PTC) was determined by HPLC analysis of fMetPhe. B. Translocation was monitored by the fluorescence change of fMetPhe-tRNA Phe (Prf16/17). Curve 1 – control ribosomes; curve 2 – colicin E3-cleaved ribosomes; curve 3 – control ribosomes in the presence of viomycin (200 μM); curve 4 – colicin E3-cleaved ribosomes with viomycin (200 μM). Normalized ΔF, fluorescence change normalized by the maximum extent of translocation determined by the Pmn reaction. C. Pi release upon GTP hydrolysis by EF-G (curves 1 and 2) or buffer control (curves 3 and 4) with control ribosomes (curves 1 and 3) or colicin E3-cleaved (curves 2 and 4). Pi release was measured by the fluorescence change of MDCC-PBP upon Pi binding ( Experimental procedures ). D. Multiple-turnover GTP hydrolysis by EF-G. Velocity of GTP hydrolysis was measured with catalytic concentrations of EF-G (10 nM) and increasing concentrations of colicin E3-cleaved ribosomes (closed circles) or control ribosomes (open circles) in the presence of excess [γ- 32 P]-GTP (200 μM).

    Journal: Molecular Microbiology

    Article Title: Colicin E3 cleavage of 16S rRNA impairs decoding and accelerates tRNA translocation on Escherichia coli ribosomes

    doi: 10.1111/j.1365-2958.2008.06283.x

    Figure Lengend Snippet: Translocation. A. Colicin E3-cleaved (closed circles) or control (open circles) pre-translocation complexes (0.1 μM) were mixed in a quench-flow apparatus with EF-G·GTP (3 μM) and Pmn (10 mM) and translocation analysed by formation of fMetPhe-Pmn. The amount of pre-translocation complex (PTC) was determined by HPLC analysis of fMetPhe. B. Translocation was monitored by the fluorescence change of fMetPhe-tRNA Phe (Prf16/17). Curve 1 – control ribosomes; curve 2 – colicin E3-cleaved ribosomes; curve 3 – control ribosomes in the presence of viomycin (200 μM); curve 4 – colicin E3-cleaved ribosomes with viomycin (200 μM). Normalized ΔF, fluorescence change normalized by the maximum extent of translocation determined by the Pmn reaction. C. Pi release upon GTP hydrolysis by EF-G (curves 1 and 2) or buffer control (curves 3 and 4) with control ribosomes (curves 1 and 3) or colicin E3-cleaved (curves 2 and 4). Pi release was measured by the fluorescence change of MDCC-PBP upon Pi binding ( Experimental procedures ). D. Multiple-turnover GTP hydrolysis by EF-G. Velocity of GTP hydrolysis was measured with catalytic concentrations of EF-G (10 nM) and increasing concentrations of colicin E3-cleaved ribosomes (closed circles) or control ribosomes (open circles) in the presence of excess [γ- 32 P]-GTP (200 μM).

    Article Snippet: The amount of fMetPhe formed was determined by reversed-phase HPLC (Lichrospher 100 RP-8, Merck).

    Techniques: Translocation Assay, Flow Cytometry, High Performance Liquid Chromatography, Fluorescence, Binding Assay

    Distinct HRNR-derived CIDAMPs show similar ribosomal protein binding patterns. ( a ) SulfoLink®–column-bound proteins of an E . coli -extract were separated on a Jupiter® C18 RP-HPLC column with a Prp-gradient. HPLC fractions containing UV-absorbing peaks (C1–D10) were divided into five aliquots and adjusted in parallel to five PAGE-gels and separated. ( b ) Silver-stained proteins. ( c ) HRNR-Far-Western blot for probing with biotinylated HR1-18 (HRNR 2556–2677 ) using Strep - Tactin ®, ( d ) HRNR-Far-Western blot for probing with biotinylated rSumo3-HRNR 2591–2684 using Strep - Tactin ®, ( e ) HRNR-Far-Western blot for probing with rHRNR 2591–2684 using anti-HRNR 2591–2684 antibodies, ( f ) HRNR-Far-Western blot for probing with rHRNR 1075–1172 using anti-HRNR 1075–1172 antibodies. Note similarities of the staining patterns, irrespective the CIDAMP AA-sequence or biotin-labeling and irrespective whether a Strep - Tactin ®- or antibody-detectable CIDAMP was used to probe and detect the target protein on the membrane. Note the presence of 70 kDa bands upon HRNR-Far-Western blot analyses in most of the investigated HPLC fractions with highest intensity for rHRNR 1075–1172 binding ( f ). The most intensive band, corresponding to a 37 kDa protein in fraction number C13, was identified as E . coli ribosomal protein L2.

    Journal: Scientific Reports

    Article Title: Hornerin contains a Linked Series of Ribosome-Targeting Peptide Antibiotics

    doi: 10.1038/s41598-018-34467-8

    Figure Lengend Snippet: Distinct HRNR-derived CIDAMPs show similar ribosomal protein binding patterns. ( a ) SulfoLink®–column-bound proteins of an E . coli -extract were separated on a Jupiter® C18 RP-HPLC column with a Prp-gradient. HPLC fractions containing UV-absorbing peaks (C1–D10) were divided into five aliquots and adjusted in parallel to five PAGE-gels and separated. ( b ) Silver-stained proteins. ( c ) HRNR-Far-Western blot for probing with biotinylated HR1-18 (HRNR 2556–2677 ) using Strep - Tactin ®, ( d ) HRNR-Far-Western blot for probing with biotinylated rSumo3-HRNR 2591–2684 using Strep - Tactin ®, ( e ) HRNR-Far-Western blot for probing with rHRNR 2591–2684 using anti-HRNR 2591–2684 antibodies, ( f ) HRNR-Far-Western blot for probing with rHRNR 1075–1172 using anti-HRNR 1075–1172 antibodies. Note similarities of the staining patterns, irrespective the CIDAMP AA-sequence or biotin-labeling and irrespective whether a Strep - Tactin ®- or antibody-detectable CIDAMP was used to probe and detect the target protein on the membrane. Note the presence of 70 kDa bands upon HRNR-Far-Western blot analyses in most of the investigated HPLC fractions with highest intensity for rHRNR 1075–1172 binding ( f ). The most intensive band, corresponding to a 37 kDa protein in fraction number C13, was identified as E . coli ribosomal protein L2.

    Article Snippet: We either used a Jupiter® 300 Å, 250 × 12.6 mm, C18-RP-HPLC column (Phenomenex) or an Aeris® widepore XB C18, 250 × 12.6 mm, RP-HPLC column (Phenomenex) and either a gradient of acetonitrile (ACN) in aqueous 0.1% TFA, or a gradient of 2-propanol (Prp) in aqueous 0.1% TFA – as indicated for separation of ribosomal proteins.

    Techniques: Derivative Assay, Protein Binding, High Performance Liquid Chromatography, Polyacrylamide Gel Electrophoresis, Staining, Far Western Blot, Sequencing, Labeling, Binding Assay

    Recombinant production of Mb1a. Semi-preparative RP-HPLC chromatogram of recombinant Mb1a released by TEV protease cleavage of the MBP-Mb1a fusion protein (see Materials and Methods for more details). The dotted line indicates the gradient of solvent B (90% acetonitrile/0.043% TFA). Top inset: SDS-PAGE gel showing pre-cleaved MBP-Mb1a fusion protein (lane 1) and remaining MBP after cleavage (lane 2). Lane M contains molecular markers (masses in kDa). Bottom inset: MALDI-TOF mass spectrum of pure recombinant Mb1a.

    Journal: Toxins

    Article Title: Insect-Active Toxins with Promiscuous Pharmacology from the African Theraphosid Spider Monocentropus balfouri

    doi: 10.3390/toxins9050155

    Figure Lengend Snippet: Recombinant production of Mb1a. Semi-preparative RP-HPLC chromatogram of recombinant Mb1a released by TEV protease cleavage of the MBP-Mb1a fusion protein (see Materials and Methods for more details). The dotted line indicates the gradient of solvent B (90% acetonitrile/0.043% TFA). Top inset: SDS-PAGE gel showing pre-cleaved MBP-Mb1a fusion protein (lane 1) and remaining MBP after cleavage (lane 2). Lane M contains molecular markers (masses in kDa). Bottom inset: MALDI-TOF mass spectrum of pure recombinant Mb1a.

    Article Snippet: The supernatant was filtered with a 0.45 μm syringe filter (EMD Millipore, Billerica, MA, USA) before purification of recombinant Mb1a or Mb1b using semi-preparative RP-HPLC (Phenomenex Jupiter C4 column; 250 × 10 mm, 10 μm; flow rate 5 mL/min).

    Techniques: Recombinant, High Performance Liquid Chromatography, SDS Page

    ( a ) Photo of a female M. balfouri ; ( b ) Chromatogram resulting from RP-HPLC fractionation of M. balfouri venom. The peak highlighted in red contains the µ/ω-TRTX-Mb1a/b peptide. The dotted line indicates the gradient of solvent B (90% acetonitrile/0.1% formic acid). Inset is a MALDI-TOF mass spectrum of the isolated µ/ω-TRTX-Mb1a/b peptide.

    Journal: Toxins

    Article Title: Insect-Active Toxins with Promiscuous Pharmacology from the African Theraphosid Spider Monocentropus balfouri

    doi: 10.3390/toxins9050155

    Figure Lengend Snippet: ( a ) Photo of a female M. balfouri ; ( b ) Chromatogram resulting from RP-HPLC fractionation of M. balfouri venom. The peak highlighted in red contains the µ/ω-TRTX-Mb1a/b peptide. The dotted line indicates the gradient of solvent B (90% acetonitrile/0.1% formic acid). Inset is a MALDI-TOF mass spectrum of the isolated µ/ω-TRTX-Mb1a/b peptide.

    Article Snippet: The supernatant was filtered with a 0.45 μm syringe filter (EMD Millipore, Billerica, MA, USA) before purification of recombinant Mb1a or Mb1b using semi-preparative RP-HPLC (Phenomenex Jupiter C4 column; 250 × 10 mm, 10 μm; flow rate 5 mL/min).

    Techniques: High Performance Liquid Chromatography, Fractionation, Isolation

    Isolation of vurtoxin and Vur-S49 by reverse-phase HPLC. Separation was done on a Discovery BIO Wide Pore C18 column (10×250 mm, Supelco) in a gradient of 25–40% (v/v) acetonitrile in 60 min in the presence of 0.1% (v/v) trifluoroacetic acid, at a flow rate of 2.0 ml/min. Fraction containing Vur-S49 (4) and vurtoxin (11) are indicated by horizontal bars.

    Journal: PLoS ONE

    Article Title: Inhibition of Nicotinic Acetylcholine Receptors, a Novel Facet in the Pleiotropic Activities of Snake Venom Phospholipases A2

    doi: 10.1371/journal.pone.0115428

    Figure Lengend Snippet: Isolation of vurtoxin and Vur-S49 by reverse-phase HPLC. Separation was done on a Discovery BIO Wide Pore C18 column (10×250 mm, Supelco) in a gradient of 25–40% (v/v) acetonitrile in 60 min in the presence of 0.1% (v/v) trifluoroacetic acid, at a flow rate of 2.0 ml/min. Fraction containing Vur-S49 (4) and vurtoxin (11) are indicated by horizontal bars.

    Article Snippet: Fraction 3+4 ( in ) was further purified by reversed phase HPLC on a Discovery BIO Wide Pore C18 column (10×250 mm, Supelco) in a gradient of 25–40% (v/v) acetonitrile in 60 min in the presence of 0.1% (v/v) trifluoroacetic acid, at a flow rate of 2.0 ml/min ( ).

    Techniques: Isolation, High Performance Liquid Chromatography, Flow Cytometry

    Effect of DB3 and DB3DB3 on different Aβ aggregation species. A) Analysis of Aβ(1–42) aggregation species with density gradient centrifugation and followed by analysis using silver-stained Tricine-SDS-PAGE to analyze the influence of DB3 and DB3DB3 on the distribution of Aβ assemblies. B) Quantification of Aβ(1–42) by RP-HPLC. All data were recorded in triplicate.

    Journal: PLoS ONE

    Article Title: Optimization of the All-D Peptide D3 for Aβ Oligomer Elimination

    doi: 10.1371/journal.pone.0153035

    Figure Lengend Snippet: Effect of DB3 and DB3DB3 on different Aβ aggregation species. A) Analysis of Aβ(1–42) aggregation species with density gradient centrifugation and followed by analysis using silver-stained Tricine-SDS-PAGE to analyze the influence of DB3 and DB3DB3 on the distribution of Aβ assemblies. B) Quantification of Aβ(1–42) by RP-HPLC. All data were recorded in triplicate.

    Article Snippet: For quantification of the Aβ(1–42) amount in each fraction, reversed-phase high performance liquid chromatography (RP-HPLC) was performed using a Zorbax SB-300 C8 column (Agilent, Böblingen, Germany) connected to an Agilent 1260 Infinity system using 30% (v/v) acetonitrile with 0.1% (v/v) trifluoroacetic acid (TFA) as the mobile phase with a flow of 1 ml/min and a column temperature of 80°C.

    Techniques: Gradient Centrifugation, Staining, SDS Page, High Performance Liquid Chromatography

    LOX-mediated oxidation of PU-NAEs. Oxidation of PU-NAEs relative to PU-FFA by heterologously expressed AtLOX1–6 , to their corresponding hydroperoxides (and chemical reduction to hydroxides), is shown in A . The products NAE-HOD and NAE-HOT were further separated on NP-HPLC to identify the preferred position of oxygenation ( B and C , respectively). Error bars show the standard deviation of three independent experiments.

    Journal: The Journal of Biological Chemistry

    Article Title: Lipoxygenase-mediated Oxidation of Polyunsaturated N-Acylethanolamines in Arabidopsis *

    doi: 10.1074/jbc.M110.217588

    Figure Lengend Snippet: LOX-mediated oxidation of PU-NAEs. Oxidation of PU-NAEs relative to PU-FFA by heterologously expressed AtLOX1–6 , to their corresponding hydroperoxides (and chemical reduction to hydroxides), is shown in A . The products NAE-HOD and NAE-HOT were further separated on NP-HPLC to identify the preferred position of oxygenation ( B and C , respectively). Error bars show the standard deviation of three independent experiments.

    Article Snippet: NAE-LOX products were separated by RP-HPLC (EC 250/2 Nucleodure 100-5 C18ec column, 250 mm × 2.1 mm, 5-μm particle size; Macherey-Nagel, Düren, Germany).

    Techniques: Normal Phase Liquid Chromatography, Standard Deviation

    Separation of NAE- and free-oxylipins. LOX products generated in vitro , with and without reduction, from PU-NAEs and FFAs, using 13-GmLOX and 9-StLOX enzymes were separated on RP-HPLC ( A ). mAU, milli-absorbance units. Fractions eluted from RP that were generated from PU-NAEs were pooled together and further separated on NP ( B ). All the fractions eluted on RP- and NP-HPLC were identified by GC/LC-MS. Norm , normalized.

    Journal: The Journal of Biological Chemistry

    Article Title: Lipoxygenase-mediated Oxidation of Polyunsaturated N-Acylethanolamines in Arabidopsis *

    doi: 10.1074/jbc.M110.217588

    Figure Lengend Snippet: Separation of NAE- and free-oxylipins. LOX products generated in vitro , with and without reduction, from PU-NAEs and FFAs, using 13-GmLOX and 9-StLOX enzymes were separated on RP-HPLC ( A ). mAU, milli-absorbance units. Fractions eluted from RP that were generated from PU-NAEs were pooled together and further separated on NP ( B ). All the fractions eluted on RP- and NP-HPLC were identified by GC/LC-MS. Norm , normalized.

    Article Snippet: NAE-LOX products were separated by RP-HPLC (EC 250/2 Nucleodure 100-5 C18ec column, 250 mm × 2.1 mm, 5-μm particle size; Macherey-Nagel, Düren, Germany).

    Techniques: Generated, In Vitro, High Performance Liquid Chromatography, Normal Phase Liquid Chromatography, Liquid Chromatography with Mass Spectroscopy

    Identification of endogenous NAE-oxylipins. Lipid extractions of 4-day-old FAAH KO seedlings showed evidence for endogenous 13NAE-HOD and 9NAE-HOD. Products were separated on reverse and normal phase HPLC and identified as TMS-derivatives by GC-MS. Characteristic mass fragmentation pattern for 13/9NAE-HOD is shown.

    Journal: The Journal of Biological Chemistry

    Article Title: Lipoxygenase-mediated Oxidation of Polyunsaturated N-Acylethanolamines in Arabidopsis *

    doi: 10.1074/jbc.M110.217588

    Figure Lengend Snippet: Identification of endogenous NAE-oxylipins. Lipid extractions of 4-day-old FAAH KO seedlings showed evidence for endogenous 13NAE-HOD and 9NAE-HOD. Products were separated on reverse and normal phase HPLC and identified as TMS-derivatives by GC-MS. Characteristic mass fragmentation pattern for 13/9NAE-HOD is shown.

    Article Snippet: NAE-LOX products were separated by RP-HPLC (EC 250/2 Nucleodure 100-5 C18ec column, 250 mm × 2.1 mm, 5-μm particle size; Macherey-Nagel, Düren, Germany).

    Techniques: High Performance Liquid Chromatography, Gas Chromatography-Mass Spectrometry

    HPLC profiles on a C-18 analytical column of 1 as reference (top) and of aliquots withdrawn from incubation of the nucleopeptide in 94% fresh human serum at 37 °C at different times (detection at 260 nm).

    Journal: Rsc Advances

    Article Title: Solid phase synthesis and RNA-binding activity of an arginine-containing nucleopeptide phase synthesis and RNA-binding activity of an arginine-containing nucleopeptide †Electronic supplementary information (ESI) available. See DOI: 10.1039/c5ra25809jClick here for additional data file.

    doi: 10.1039/c5ra25809j

    Figure Lengend Snippet: HPLC profiles on a C-18 analytical column of 1 as reference (top) and of aliquots withdrawn from incubation of the nucleopeptide in 94% fresh human serum at 37 °C at different times (detection at 260 nm).

    Article Snippet: The nucleopeptide was then purified by RP-HPLC using a linear gradient of 10% (for 5 min) to 30% B in A over 30 min: t R = 20.0 min. After lyophilisation, the purified product was dissolved in a known amount of milliQ water and quantified by UV measurements at 260 nm giving 2.2 μmol of 1 (55% yield); the compound was ≥95% pure by HPLC analysis.

    Techniques: High Performance Liquid Chromatography, Incubation