acetonitril acn Search Results


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  • 99
    Thermo Fisher acetonitrile acn
    MALDI mass spectra of purified rice-derived rhTF (a close-up view). The apo- rhTFs was desalted using ZipTip ™ <t>μ-C18</t> pipette tips (Millipore, Billerica, MA), eluted with a solution of 70% acetonitrile <t>(ACN),</t> 0.2% formic acid, and 5 mg/ml MALDI matrix (α-cyano-4-hydroxycinnamic acid), and analyzed with an Applied Biosystems 4700 Proteomics Analyzer.
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    Millipore acetonitrile acn
    Example of <t>PDA</t> reactivity. (i) Glutaraldehyde reactivity to 0.1 mM PDA was observed with (a) 1 mM, (b) 2 mM, (c) 4 mM, (d) 8 Mm and (e) 10 mM glutaraldehyde in 50:50 <t>ACN:PB</t> (pH 7.4). (ii) PDA (0.1 mM) was reacted with (a) 1, (b) 2, (c) 4, and (d) 8 mM
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    93
    Fisher Scientific acetonitrile acn
    Chromatographic separation of (A) 18 SPMs (100 nM each) and (B) 5 deuterated internal standards (20 nM) covered by the method including (C) DHA derived D-series resolvins, (D) EPA derived E-series resolvins, (E) EPA and ARA derived lipoxins, DHA derived (F) protectins, and (G) maresins. Separation was carried out on an RP-18 column (2.1 × 150 mm, particle size 1.8 μm, pore size 9.5 nm) with a H 2 <t>O/MeOH/ACN/HAc</t> gradient.
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    93
    Merck KGaA acetonitrile acn
    <t>HPLC</t> profiles of the fragmentation of LK by selected Saps. LK samples (1.5 μM) were digested with 0.03 μM of Sap1, −3, −4, −8, and −9 in the citrate buffer (pH 5.0) at 37°C for 24 hours. The reaction was stopped using pepstatin A (10 μM), followed by acidification with HCl (0.33 M). The samples were analyzed using HPLC on the Luna C18(2) 5 μm 4.6 × 250 mm column (Phenomenex) in a TFA <t>water-ACN</t> binary gradient system, as described in the Materials and Methods section. Arrows indicate the retention times of the Met-Lys-bradykinin (M) and des-Arg 1 -bradykinin (D) standards.
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    93
    Avantor acetonitrile acn
    Separation of the enantiomers of RS/SR phenylpropanolamine (Solute #26 in Table 1 ) on a 25 cm Larihc CF6-P column in PO mode with (A) <t>ACN/</t> <t>MeOH/TFA/TEA</t> (90:10:0.3:0.2, v/v/v/v) and (B) ACN/MeOH/AA/TEA (60:40:0.3:0.2, v/v/v/v). Flow rate: 2 mL/min; detection UV: 254 nm.
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    Biosolve acetonitrile acn
    Separation of the enantiomers of RS/SR phenylpropanolamine (Solute #26 in Table 1 ) on a 25 cm Larihc CF6-P column in PO mode with (A) <t>ACN/</t> <t>MeOH/TFA/TEA</t> (90:10:0.3:0.2, v/v/v/v) and (B) ACN/MeOH/AA/TEA (60:40:0.3:0.2, v/v/v/v). Flow rate: 2 mL/min; detection UV: 254 nm.
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    92
    Fisher Scientific hplc grade acetonitrile acn
    Representative comparison of analytical <t>HPLC</t> chromatograms from various RPIP conditions eluting persulfated N -cbz neomycin. Each chromatogram was generated from a 20 min. gradient increase in percent <t>ACN,</t> and the ending percent ACN was then maintained
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    93
    Burdick & Jackson acetonitrile acn
    <t>HPLC</t> chromatograms: ( a ) condition 1 with Agilent XDB-C18 at an isocratic mobile phase of acetonitrile <t>(ACN):water</t> (0.7% trifluoroacetic acid (TFA), 5 mM heptafluorobutyric acid (HFBA)) = 2:98; ( b ) condition 2 with YMC Triart-C8 at an isocratic mobile phase of ACN:water (0.7% TFA, 5 mM HFBA) = 2:98; ( c ) condition 3 with YMC Triart-C8 at an isocratic mobile phase of ACN:water (0.7% TFA, 5 mM HFBA) = 9:91; ( d ) after approximately 48 hours of repeated measurements with condition 3.
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    99
    Millipore hplc grade acetonitrile acn
    <t>HPLC</t> chromatograms: ( a ) condition 1 with Agilent XDB-C18 at an isocratic mobile phase of acetonitrile <t>(ACN):water</t> (0.7% trifluoroacetic acid (TFA), 5 mM heptafluorobutyric acid (HFBA)) = 2:98; ( b ) condition 2 with YMC Triart-C8 at an isocratic mobile phase of ACN:water (0.7% TFA, 5 mM HFBA) = 2:98; ( c ) condition 3 with YMC Triart-C8 at an isocratic mobile phase of ACN:water (0.7% TFA, 5 mM HFBA) = 9:91; ( d ) after approximately 48 hours of repeated measurements with condition 3.
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    92
    Merck & Co acetonitrile acn
    <t>HPLC</t> chromatograms: ( a ) condition 1 with Agilent XDB-C18 at an isocratic mobile phase of acetonitrile <t>(ACN):water</t> (0.7% trifluoroacetic acid (TFA), 5 mM heptafluorobutyric acid (HFBA)) = 2:98; ( b ) condition 2 with YMC Triart-C8 at an isocratic mobile phase of ACN:water (0.7% TFA, 5 mM HFBA) = 2:98; ( c ) condition 3 with YMC Triart-C8 at an isocratic mobile phase of ACN:water (0.7% TFA, 5 mM HFBA) = 9:91; ( d ) after approximately 48 hours of repeated measurements with condition 3.
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    92
    Tedia acetonitrile acn
    RP-HPLC analysis of PEGylated HM-3. Analysis was performed on a C18 column with <t>water/ACN/TFA</t> as eluent and a flow rate of 1 mL/min, and peaks were monitored at 220 nm. ( A ) ALD-mPEG 5k -HM-3 purity: 97.39%, T: 9.395 min; ( B ) ALD-mPEG 10k -HM-3 purity: 98.23%, T: 9.698 min; ( C ) SC-mPEG 10k -HM-3 purity: 97.02%, T: 9.883 min; ( D ) SC-mPEG 20k -HM-3 purity: 98.52%, T: 9.578 min.
    Acetonitrile Acn, supplied by Tedia, used in various techniques. Bioz Stars score: 92/100, based on 53 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Merck KGaA hplc grade acetonitrile acn
    RP-HPLC analysis of PEGylated HM-3. Analysis was performed on a C18 column with <t>water/ACN/TFA</t> as eluent and a flow rate of 1 mL/min, and peaks were monitored at 220 nm. ( A ) ALD-mPEG 5k -HM-3 purity: 97.39%, T: 9.395 min; ( B ) ALD-mPEG 10k -HM-3 purity: 98.23%, T: 9.698 min; ( C ) SC-mPEG 10k -HM-3 purity: 97.02%, T: 9.883 min; ( D ) SC-mPEG 20k -HM-3 purity: 98.52%, T: 9.578 min.
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    92
    Waters Corporation acetonitrile acn
    RP-HPLC analysis of PEGylated HM-3. Analysis was performed on a C18 column with <t>water/ACN/TFA</t> as eluent and a flow rate of 1 mL/min, and peaks were monitored at 220 nm. ( A ) ALD-mPEG 5k -HM-3 purity: 97.39%, T: 9.395 min; ( B ) ALD-mPEG 10k -HM-3 purity: 98.23%, T: 9.698 min; ( C ) SC-mPEG 10k -HM-3 purity: 97.02%, T: 9.883 min; ( D ) SC-mPEG 20k -HM-3 purity: 98.52%, T: 9.578 min.
    Acetonitrile Acn, supplied by Waters Corporation, used in various techniques. Bioz Stars score: 92/100, based on 308 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Burdick & Jackson hplc grade acetonitrile acn
    The UV spectrum and <t>HPLC</t> chromatogram of the oyster hydrolysate solution with different initial concentration and 5% final concentration of organic solvent for 40 min in the gradient model: (a) 0.1% TFA; (b) 0.1% TFA/ 0.8% <t>ACN;</t> (c) 0.1% TFA/1% ACN. TFA, trifluoroacetic acid; ACN, acetonitrile.
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    92
    Agilent technologies acetonitrile acn
    The UV spectrum and <t>HPLC</t> chromatogram of the oyster hydrolysate solution with different initial concentration and 5% final concentration of organic solvent for 40 min in the gradient model: (a) 0.1% TFA; (b) 0.1% TFA/ 0.8% <t>ACN;</t> (c) 0.1% TFA/1% ACN. TFA, trifluoroacetic acid; ACN, acetonitrile.
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    84
    Thermo Fisher pierce acetonitrile acn lc ms grade
    The UV spectrum and <t>HPLC</t> chromatogram of the oyster hydrolysate solution with different initial concentration and 5% final concentration of organic solvent for 40 min in the gradient model: (a) 0.1% TFA; (b) 0.1% TFA/ 0.8% <t>ACN;</t> (c) 0.1% TFA/1% ACN. TFA, trifluoroacetic acid; ACN, acetonitrile.
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    92
    Avantor hplc grade acetonitrile acn
    Detection of Cleaved Substrate Peptide by Mass Spectrometry A-B. 10 ng of recombinant AEP (rAEP) was incubated with 1 μg (0.65 mM) synthetic substrate peptide (hpvFAANDVSKvph) overnight at 37°C. Samples were dried down by vacuum centrifuge and resuspended in LB. 5 pmole of the substrate was loaded on to the liquid chromatography column and cleaved substrate was analysed by SRM MS (A) followed by an DDA workflow (B). (A) Three SRM transitions (b4-481.25 + , b5-552.29 + , b6-623.33 + ) were used to detect the cleaved substrate, sequenced as hpvFAAN (378.2 2+ precursor ion). The target peptide eluted at 32 min during the chromatographic gradient. (B) Product ion scans of precursor 378.2 2+ as analysed by DDA. C. Synthetic peptide sequenced as cleaved form of the substrate (hpvFAAN) was dissolved into <t>HPLC</t> grade water and seven different concentrations from 1 amole to 1 pmole were made in loading buffer (LB), containing 20 mM citric acid, 0.1% FA, 0.1% <t>ACN.</t> D. 10 amole, 100 amole, 1 fmole, 10 fmole, or 100 fmole of the substrate (hpvFAAN) peptide was spiked into normal plasma. Samples were precipitated using 2 volumes of ACN and dried down using vacuum centrifugation. Samples were resuspended in LB and analyzed by SRM MS. Error bars shown are +/−SEM (n = 3).
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    92
    honeywell international acetonitrile acn
    Detection of Cleaved Substrate Peptide by Mass Spectrometry A-B. 10 ng of recombinant AEP (rAEP) was incubated with 1 μg (0.65 mM) synthetic substrate peptide (hpvFAANDVSKvph) overnight at 37°C. Samples were dried down by vacuum centrifuge and resuspended in LB. 5 pmole of the substrate was loaded on to the liquid chromatography column and cleaved substrate was analysed by SRM MS (A) followed by an DDA workflow (B). (A) Three SRM transitions (b4-481.25 + , b5-552.29 + , b6-623.33 + ) were used to detect the cleaved substrate, sequenced as hpvFAAN (378.2 2+ precursor ion). The target peptide eluted at 32 min during the chromatographic gradient. (B) Product ion scans of precursor 378.2 2+ as analysed by DDA. C. Synthetic peptide sequenced as cleaved form of the substrate (hpvFAAN) was dissolved into <t>HPLC</t> grade water and seven different concentrations from 1 amole to 1 pmole were made in loading buffer (LB), containing 20 mM citric acid, 0.1% FA, 0.1% <t>ACN.</t> D. 10 amole, 100 amole, 1 fmole, 10 fmole, or 100 fmole of the substrate (hpvFAAN) peptide was spiked into normal plasma. Samples were precipitated using 2 volumes of ACN and dried down using vacuum centrifugation. Samples were resuspended in LB and analyzed by SRM MS. Error bars shown are +/−SEM (n = 3).
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    92
    Mallinckrodt hplc grade acetonitrile acn
    Detection of Cleaved Substrate Peptide by Mass Spectrometry A-B. 10 ng of recombinant AEP (rAEP) was incubated with 1 μg (0.65 mM) synthetic substrate peptide (hpvFAANDVSKvph) overnight at 37°C. Samples were dried down by vacuum centrifuge and resuspended in LB. 5 pmole of the substrate was loaded on to the liquid chromatography column and cleaved substrate was analysed by SRM MS (A) followed by an DDA workflow (B). (A) Three SRM transitions (b4-481.25 + , b5-552.29 + , b6-623.33 + ) were used to detect the cleaved substrate, sequenced as hpvFAAN (378.2 2+ precursor ion). The target peptide eluted at 32 min during the chromatographic gradient. (B) Product ion scans of precursor 378.2 2+ as analysed by DDA. C. Synthetic peptide sequenced as cleaved form of the substrate (hpvFAAN) was dissolved into <t>HPLC</t> grade water and seven different concentrations from 1 amole to 1 pmole were made in loading buffer (LB), containing 20 mM citric acid, 0.1% FA, 0.1% <t>ACN.</t> D. 10 amole, 100 amole, 1 fmole, 10 fmole, or 100 fmole of the substrate (hpvFAAN) peptide was spiked into normal plasma. Samples were precipitated using 2 volumes of ACN and dried down using vacuum centrifugation. Samples were resuspended in LB and analyzed by SRM MS. Error bars shown are +/−SEM (n = 3).
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    92
    RATHBURN CHEMICALS LIMITED acetonitrile acn
    Detection of Cleaved Substrate Peptide by Mass Spectrometry A-B. 10 ng of recombinant AEP (rAEP) was incubated with 1 μg (0.65 mM) synthetic substrate peptide (hpvFAANDVSKvph) overnight at 37°C. Samples were dried down by vacuum centrifuge and resuspended in LB. 5 pmole of the substrate was loaded on to the liquid chromatography column and cleaved substrate was analysed by SRM MS (A) followed by an DDA workflow (B). (A) Three SRM transitions (b4-481.25 + , b5-552.29 + , b6-623.33 + ) were used to detect the cleaved substrate, sequenced as hpvFAAN (378.2 2+ precursor ion). The target peptide eluted at 32 min during the chromatographic gradient. (B) Product ion scans of precursor 378.2 2+ as analysed by DDA. C. Synthetic peptide sequenced as cleaved form of the substrate (hpvFAAN) was dissolved into <t>HPLC</t> grade water and seven different concentrations from 1 amole to 1 pmole were made in loading buffer (LB), containing 20 mM citric acid, 0.1% FA, 0.1% <t>ACN.</t> D. 10 amole, 100 amole, 1 fmole, 10 fmole, or 100 fmole of the substrate (hpvFAAN) peptide was spiked into normal plasma. Samples were precipitated using 2 volumes of ACN and dried down using vacuum centrifugation. Samples were resuspended in LB and analyzed by SRM MS. Error bars shown are +/−SEM (n = 3).
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    Tedia hplc grade acetonitrile acn
    <t>RP-HPLC</t> separation on a capillary C18 column of the anion-exchange purified fraction containing the heteroconjugate. In (a) a gradient composed of buffer A: 5 mM ammonium acetate, 5% <t>ACN/H</t> 2 O and buffer B: 95% ACN/H 2 O was used. In (b) a gradient composed
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    Image Search Results


    MALDI mass spectra of purified rice-derived rhTF (a close-up view). The apo- rhTFs was desalted using ZipTip ™ μ-C18 pipette tips (Millipore, Billerica, MA), eluted with a solution of 70% acetonitrile (ACN), 0.2% formic acid, and 5 mg/ml MALDI matrix (α-cyano-4-hydroxycinnamic acid), and analyzed with an Applied Biosystems 4700 Proteomics Analyzer.

    Journal: Protein expression and purification

    Article Title: Expression, purification, and characterization of recombinant human transferrin from rice (Oryza sativa L.)

    doi: 10.1016/j.pep.2010.04.019

    Figure Lengend Snippet: MALDI mass spectra of purified rice-derived rhTF (a close-up view). The apo- rhTFs was desalted using ZipTip ™ μ-C18 pipette tips (Millipore, Billerica, MA), eluted with a solution of 70% acetonitrile (ACN), 0.2% formic acid, and 5 mg/ml MALDI matrix (α-cyano-4-hydroxycinnamic acid), and analyzed with an Applied Biosystems 4700 Proteomics Analyzer.

    Article Snippet: These iron-free or apo-TFs were further desalted using ZipTip™ μ-C18 pipette tips (Millipore, Billerica, MA), eluted with a solution of 70% acetonitrile (ACN), 0.2% formic acid, and 5 mg/ml MALDI matrix (α-cyano-4-hydroxycinnamic acid), and spotted onto the MALDI target and analyzed with an Applied Biosystems 4700 Proteomics Analyzer (Applied Biosystems Inc., Foster City, CA) at the Molecular Structure Facility at the University of California, Davis, CA, US.

    Techniques: Purification, Derivative Assay, Transferring

    Example of PDA reactivity. (i) Glutaraldehyde reactivity to 0.1 mM PDA was observed with (a) 1 mM, (b) 2 mM, (c) 4 mM, (d) 8 Mm and (e) 10 mM glutaraldehyde in 50:50 ACN:PB (pH 7.4). (ii) PDA (0.1 mM) was reacted with (a) 1, (b) 2, (c) 4, and (d) 8 mM

    Journal: Toxicology

    Article Title: Pyridoxylamine reactivity kinetics as an amine based nucleophile for screening electrophilic dermal sensitizers

    doi: 10.1016/j.tox.2013.11.009

    Figure Lengend Snippet: Example of PDA reactivity. (i) Glutaraldehyde reactivity to 0.1 mM PDA was observed with (a) 1 mM, (b) 2 mM, (c) 4 mM, (d) 8 Mm and (e) 10 mM glutaraldehyde in 50:50 ACN:PB (pH 7.4). (ii) PDA (0.1 mM) was reacted with (a) 1, (b) 2, (c) 4, and (d) 8 mM

    Article Snippet: Phosphate buffer, acetonitrile (ACN), pyridoxylamine dihydrochloride (PDA; CAS # 524-36-7) and all test chemicals which were reagent grade were purchased from Sigma Chemical Co. (St. Louis, MO) and Fisher Scientific (Pittsburgh, PA) and used without further purification.

    Techniques:

    Kinetic changes during JBH treatment show that G 3 H 2 and G 3 H 3 species from SeHAS HA are sequentially converted to smaller members of the H 2 and H 3 series. Aliquots (5 µL) of Wash 3 were incubated with 22 µL inactive (time-zero) or active JBH at 30°C for up to 26 h ( n = 4 except n = 3 at 26 h); values are the mean intensity ± SEM as indicated. Members of the G 0–3 H 3 (A) and G 0–3 H 2 (B) series were analyzed to monitor decreases or increases in each member as a function of increasing JBH digestion time, (G 3 H 2,3 , ●; G 2 H 2,3 , ▼; G 1 H 2,3 , ▲; G 0 H 2,3 , ■). Lines ( r 2 ≥ 0.97) for H 2,3 (solid) and G 3 H 2,3 (long dash) were calculated by linear regression or a 3-parameter hyperbolic decay function, respectively, using Sigma Plot v10. Lines for G 2 H 2,3 (short dash) and G 1 H 2,3 (dotted) are comprised of linear segments. (C) ACN fraction samples (10 μL) containing G 4 H 2 and much less or no smaller members of this G n H 2 series were incubated for up to 12 h, as indicated, with 22 µL of inactive (time-zero) or active JBH. Sequential and time-dependent changes in the levels of G 3 H 2 , G 2 H 2 , G 1 H 2 and H 2 are evident.

    Journal: Glycobiology

    Article Title: Hyaluronan synthase assembles hyaluronan on a [GlcNAc(β1,4)]n-GlcNAc(α1→)UDP primer and hyaluronan retains this residual chitin oligomer as a cap at the nonreducing end

    doi: 10.1093/glycob/cwx012

    Figure Lengend Snippet: Kinetic changes during JBH treatment show that G 3 H 2 and G 3 H 3 species from SeHAS HA are sequentially converted to smaller members of the H 2 and H 3 series. Aliquots (5 µL) of Wash 3 were incubated with 22 µL inactive (time-zero) or active JBH at 30°C for up to 26 h ( n = 4 except n = 3 at 26 h); values are the mean intensity ± SEM as indicated. Members of the G 0–3 H 3 (A) and G 0–3 H 2 (B) series were analyzed to monitor decreases or increases in each member as a function of increasing JBH digestion time, (G 3 H 2,3 , ●; G 2 H 2,3 , ▼; G 1 H 2,3 , ▲; G 0 H 2,3 , ■). Lines ( r 2 ≥ 0.97) for H 2,3 (solid) and G 3 H 2,3 (long dash) were calculated by linear regression or a 3-parameter hyperbolic decay function, respectively, using Sigma Plot v10. Lines for G 2 H 2,3 (short dash) and G 1 H 2,3 (dotted) are comprised of linear segments. (C) ACN fraction samples (10 μL) containing G 4 H 2 and much less or no smaller members of this G n H 2 series were incubated for up to 12 h, as indicated, with 22 µL of inactive (time-zero) or active JBH. Sequential and time-dependent changes in the levels of G 3 H 2 , G 2 H 2 , G 1 H 2 and H 2 are evident.

    Article Snippet: Jack bean β-N-acetylhexosaminidase (JBH, #A2264), Streptomyces hyalurolyticus hyaluronidase (HA lyase, #H1136), OTH (#H-6254), and ACN (HPLC grade) were from Sigma-Aldrich (St. Louis, MO).

    Techniques: Incubation

    JBH digestion of G n H n species from SeHAS HA releases nondehydro NR-end H 2 and H 3 oligos. A–F. Selected m/z ranges are shown for Wash 3 (0.5 μL) samples treated overnight at 30°C with inactive (A, C, E) or active (B, D, F) JBH and analyzed by MALDI-TOF MS in negative mode. G n H n species that decrease or increase, with active JBH treatment, are indicated in italic or boldface font, respectively. New m/z signals are evident corresponding to H 2 (B compared to A), H 3 (D compared to C) and H 4 (F compared to E). (G–J) ACN samples (1, 2 or 3 µL), as indicated, were incubated overnight at 30°C with active or inactive JBH, and the presence of m / z signals, proportionally increasing with sample volume, was monitored for H 2 (panel G) or H 3 (panel H). The m / z signal decreases for the larger G 4 H 3 (I) and G 4 H 2 (J) ions were assessed in the 3 µL samples, treated with active (top) or inactive (bottom) JBH.

    Journal: Glycobiology

    Article Title: Hyaluronan synthase assembles hyaluronan on a [GlcNAc(β1,4)]n-GlcNAc(α1→)UDP primer and hyaluronan retains this residual chitin oligomer as a cap at the nonreducing end

    doi: 10.1093/glycob/cwx012

    Figure Lengend Snippet: JBH digestion of G n H n species from SeHAS HA releases nondehydro NR-end H 2 and H 3 oligos. A–F. Selected m/z ranges are shown for Wash 3 (0.5 μL) samples treated overnight at 30°C with inactive (A, C, E) or active (B, D, F) JBH and analyzed by MALDI-TOF MS in negative mode. G n H n species that decrease or increase, with active JBH treatment, are indicated in italic or boldface font, respectively. New m/z signals are evident corresponding to H 2 (B compared to A), H 3 (D compared to C) and H 4 (F compared to E). (G–J) ACN samples (1, 2 or 3 µL), as indicated, were incubated overnight at 30°C with active or inactive JBH, and the presence of m / z signals, proportionally increasing with sample volume, was monitored for H 2 (panel G) or H 3 (panel H). The m / z signal decreases for the larger G 4 H 3 (I) and G 4 H 2 (J) ions were assessed in the 3 µL samples, treated with active (top) or inactive (bottom) JBH.

    Article Snippet: Jack bean β-N-acetylhexosaminidase (JBH, #A2264), Streptomyces hyalurolyticus hyaluronidase (HA lyase, #H1136), OTH (#H-6254), and ACN (HPLC grade) were from Sigma-Aldrich (St. Louis, MO).

    Techniques: Mass Spectrometry, Incubation

    Chromatographic separation of (A) 18 SPMs (100 nM each) and (B) 5 deuterated internal standards (20 nM) covered by the method including (C) DHA derived D-series resolvins, (D) EPA derived E-series resolvins, (E) EPA and ARA derived lipoxins, DHA derived (F) protectins, and (G) maresins. Separation was carried out on an RP-18 column (2.1 × 150 mm, particle size 1.8 μm, pore size 9.5 nm) with a H 2 O/MeOH/ACN/HAc gradient.

    Journal: Frontiers in Pharmacology

    Article Title: Development of an Optimized LC-MS Method for the Detection of Specialized Pro-Resolving Mediators in Biological Samples

    doi: 10.3389/fphar.2019.00169

    Figure Lengend Snippet: Chromatographic separation of (A) 18 SPMs (100 nM each) and (B) 5 deuterated internal standards (20 nM) covered by the method including (C) DHA derived D-series resolvins, (D) EPA derived E-series resolvins, (E) EPA and ARA derived lipoxins, DHA derived (F) protectins, and (G) maresins. Separation was carried out on an RP-18 column (2.1 × 150 mm, particle size 1.8 μm, pore size 9.5 nm) with a H 2 O/MeOH/ACN/HAc gradient.

    Article Snippet: Acetonitrile (ACN), LC-MS grade methanol (MeOH) and acetic acid were obtained from Fisher Scientific (Schwerte, Germany).

    Techniques: Derivative Assay, Acetylene Reduction Assay, HAC Assay

    HPLC profiles of the fragmentation of LK by selected Saps. LK samples (1.5 μM) were digested with 0.03 μM of Sap1, −3, −4, −8, and −9 in the citrate buffer (pH 5.0) at 37°C for 24 hours. The reaction was stopped using pepstatin A (10 μM), followed by acidification with HCl (0.33 M). The samples were analyzed using HPLC on the Luna C18(2) 5 μm 4.6 × 250 mm column (Phenomenex) in a TFA water-ACN binary gradient system, as described in the Materials and Methods section. Arrows indicate the retention times of the Met-Lys-bradykinin (M) and des-Arg 1 -bradykinin (D) standards.

    Journal: BMC Microbiology

    Article Title: Kinin release from human kininogen by 10 aspartic proteases produced by pathogenic yeast Candida albicans

    doi: 10.1186/s12866-015-0394-8

    Figure Lengend Snippet: HPLC profiles of the fragmentation of LK by selected Saps. LK samples (1.5 μM) were digested with 0.03 μM of Sap1, −3, −4, −8, and −9 in the citrate buffer (pH 5.0) at 37°C for 24 hours. The reaction was stopped using pepstatin A (10 μM), followed by acidification with HCl (0.33 M). The samples were analyzed using HPLC on the Luna C18(2) 5 μm 4.6 × 250 mm column (Phenomenex) in a TFA water-ACN binary gradient system, as described in the Materials and Methods section. Arrows indicate the retention times of the Met-Lys-bradykinin (M) and des-Arg 1 -bradykinin (D) standards.

    Article Snippet: Briefly, the protein bands, which were visualized using colloidal staining with Coomassie Brilliant Blue dye [ ], were excised from the gel and washed twice with 50 mM (NH4 )HCO3 in 50% acetonitrile (ACN) (HPLC gradient-grade; Merck, Darmstadt, Germany) at both room temperature and 37°C in order to remove any dye, and then reduced using 10 mM dithiothreitol (DTT) for 60 minutes at 60°C, alkylated with 55 mM iodoacetamide for 45 minutes at room temperature in the dark, washed with 100 mM (NH4 )HCO3 , and dehydrated with ACN.

    Techniques: High Performance Liquid Chromatography

    Distribution of bradykinin, Met-Lys-bradykinin, and des-Arg 1 -bradykinin in the Sap-digested LK samples. LK samples (1.5 μM) were digested using 0.03 μM Sap in the citrate buffer (pH 5.0) at 37°C for 6 hours. After sequentially stopping the reaction using pepstatin A and HCl, the obtained peptide mixtures were separated on the Luna C18 column in a TFA water-ACN binary gradient system. The fractions were collected at the retention times that correspond to the bradykinin, Met-Lys-bradykinin, and des-Arg 1 -bradykinin standards, evaporated to dryness, and redissolved in the assay buffer of the ELISA kit in order to quantitatively determine the kinin concentrations. The corresponding fractions, obtained from the HPLC separation of intact (undigested) LK served as the controls, and the kinin concentrations, determined in these fractions are subtracted from those in the Sap-digested LK samples. The corrected amount of each of the three kinins is expressed relative to the maximum possible amount of all kinins (as calculated using the molarity of LK in the sample). Results, obtained from two independent experiments (two LK-digests independently analyzed by HPLC for each Sap), with three replicate ELISA measurements (in three different wells) for each fraction obtained during each HPLC separation, are presented as the mean values ± standard deviation. Asterisks denote the statistical significance of the difference between the kinin levels in the Sap-treated and undigested LK samples (t-Student test, p

    Journal: BMC Microbiology

    Article Title: Kinin release from human kininogen by 10 aspartic proteases produced by pathogenic yeast Candida albicans

    doi: 10.1186/s12866-015-0394-8

    Figure Lengend Snippet: Distribution of bradykinin, Met-Lys-bradykinin, and des-Arg 1 -bradykinin in the Sap-digested LK samples. LK samples (1.5 μM) were digested using 0.03 μM Sap in the citrate buffer (pH 5.0) at 37°C for 6 hours. After sequentially stopping the reaction using pepstatin A and HCl, the obtained peptide mixtures were separated on the Luna C18 column in a TFA water-ACN binary gradient system. The fractions were collected at the retention times that correspond to the bradykinin, Met-Lys-bradykinin, and des-Arg 1 -bradykinin standards, evaporated to dryness, and redissolved in the assay buffer of the ELISA kit in order to quantitatively determine the kinin concentrations. The corresponding fractions, obtained from the HPLC separation of intact (undigested) LK served as the controls, and the kinin concentrations, determined in these fractions are subtracted from those in the Sap-digested LK samples. The corrected amount of each of the three kinins is expressed relative to the maximum possible amount of all kinins (as calculated using the molarity of LK in the sample). Results, obtained from two independent experiments (two LK-digests independently analyzed by HPLC for each Sap), with three replicate ELISA measurements (in three different wells) for each fraction obtained during each HPLC separation, are presented as the mean values ± standard deviation. Asterisks denote the statistical significance of the difference between the kinin levels in the Sap-treated and undigested LK samples (t-Student test, p

    Article Snippet: Briefly, the protein bands, which were visualized using colloidal staining with Coomassie Brilliant Blue dye [ ], were excised from the gel and washed twice with 50 mM (NH4 )HCO3 in 50% acetonitrile (ACN) (HPLC gradient-grade; Merck, Darmstadt, Germany) at both room temperature and 37°C in order to remove any dye, and then reduced using 10 mM dithiothreitol (DTT) for 60 minutes at 60°C, alkylated with 55 mM iodoacetamide for 45 minutes at room temperature in the dark, washed with 100 mM (NH4 )HCO3 , and dehydrated with ACN.

    Techniques: Enzyme-linked Immunosorbent Assay, High Performance Liquid Chromatography, Standard Deviation

    HPLC/MS characteristics of the Sap-catalyzed cleavage of the HK-D4 peptide. Ten μM of the synthetic peptide HK-D4 (which has the ISLMKRPPGFSPFRSSRIGEIKEET amino acid sequence) were treated with recombinant Sap1–10 in citrate (50 mM) or phosphate buffers (25 mM) at the optimal pH for the general proteolytic activity [ 26 ] of each individual Sap (specified in the figure) at an enzyme:substrate molar ratio of 1:50 for 24 hours at 37°C. The reaction was stopped using HCl, and the samples were analyzed using reversed-phase HPLC on an Eurosil Bioselect 300–5 C-18 column (Knauer) in a TFA-water-ACN binary gradient system. The fractions, which were collected at the major absorbance peaks (215 nm), were evaporated and analyzed using ESI-MS/MS in order to determine their amino acid sequence.

    Journal: BMC Microbiology

    Article Title: Kinin release from human kininogen by 10 aspartic proteases produced by pathogenic yeast Candida albicans

    doi: 10.1186/s12866-015-0394-8

    Figure Lengend Snippet: HPLC/MS characteristics of the Sap-catalyzed cleavage of the HK-D4 peptide. Ten μM of the synthetic peptide HK-D4 (which has the ISLMKRPPGFSPFRSSRIGEIKEET amino acid sequence) were treated with recombinant Sap1–10 in citrate (50 mM) or phosphate buffers (25 mM) at the optimal pH for the general proteolytic activity [ 26 ] of each individual Sap (specified in the figure) at an enzyme:substrate molar ratio of 1:50 for 24 hours at 37°C. The reaction was stopped using HCl, and the samples were analyzed using reversed-phase HPLC on an Eurosil Bioselect 300–5 C-18 column (Knauer) in a TFA-water-ACN binary gradient system. The fractions, which were collected at the major absorbance peaks (215 nm), were evaporated and analyzed using ESI-MS/MS in order to determine their amino acid sequence.

    Article Snippet: Briefly, the protein bands, which were visualized using colloidal staining with Coomassie Brilliant Blue dye [ ], were excised from the gel and washed twice with 50 mM (NH4 )HCO3 in 50% acetonitrile (ACN) (HPLC gradient-grade; Merck, Darmstadt, Germany) at both room temperature and 37°C in order to remove any dye, and then reduced using 10 mM dithiothreitol (DTT) for 60 minutes at 60°C, alkylated with 55 mM iodoacetamide for 45 minutes at room temperature in the dark, washed with 100 mM (NH4 )HCO3 , and dehydrated with ACN.

    Techniques: High Performance Liquid Chromatography, Mass Spectrometry, Sequencing, Recombinant, Activity Assay

    Separation of the enantiomers of RS/SR phenylpropanolamine (Solute #26 in Table 1 ) on a 25 cm Larihc CF6-P column in PO mode with (A) ACN/ MeOH/TFA/TEA (90:10:0.3:0.2, v/v/v/v) and (B) ACN/MeOH/AA/TEA (60:40:0.3:0.2, v/v/v/v). Flow rate: 2 mL/min; detection UV: 254 nm.

    Journal: Journal of Pharmaceutical Analysis

    Article Title: Screening primary racemic amines for enantioseparation by derivatized polysaccharide and cyclofructan columns

    doi: 10.1016/j.jpha.2016.07.003

    Figure Lengend Snippet: Separation of the enantiomers of RS/SR phenylpropanolamine (Solute #26 in Table 1 ) on a 25 cm Larihc CF6-P column in PO mode with (A) ACN/ MeOH/TFA/TEA (90:10:0.3:0.2, v/v/v/v) and (B) ACN/MeOH/AA/TEA (60:40:0.3:0.2, v/v/v/v). Flow rate: 2 mL/min; detection UV: 254 nm.

    Article Snippet: Acetonitrile (ACN), methanol (MeOH), ethanol (EtOH), n-heptane (hept), and isopropyl alcohol (IPA) of HPLC grade were obtained from VWR (Sugarland, Texas), and used as received.

    Techniques: Flow Cytometry

    Separation of the enantiomers of (±) trans-1-Amino-2-indanol (Solute #21 in Table 1 ) on a 25 cm column in PO mode as (A) ChiralPak IB column with ACN/IPA (97:3, v/v) mobile phase with 0.1% BA and (B) Larihc CF6-P column with ACN/MeOH (90:10, v/v) mobile phase with 0.3% TFA and 0.2% TEA ionic additives. Flow rate: 2 mL/min; detection UV: 254 nm.

    Journal: Journal of Pharmaceutical Analysis

    Article Title: Screening primary racemic amines for enantioseparation by derivatized polysaccharide and cyclofructan columns

    doi: 10.1016/j.jpha.2016.07.003

    Figure Lengend Snippet: Separation of the enantiomers of (±) trans-1-Amino-2-indanol (Solute #21 in Table 1 ) on a 25 cm column in PO mode as (A) ChiralPak IB column with ACN/IPA (97:3, v/v) mobile phase with 0.1% BA and (B) Larihc CF6-P column with ACN/MeOH (90:10, v/v) mobile phase with 0.3% TFA and 0.2% TEA ionic additives. Flow rate: 2 mL/min; detection UV: 254 nm.

    Article Snippet: Acetonitrile (ACN), methanol (MeOH), ethanol (EtOH), n-heptane (hept), and isopropyl alcohol (IPA) of HPLC grade were obtained from VWR (Sugarland, Texas), and used as received.

    Techniques: Indirect Immunoperoxidase Assay, Flow Cytometry

    Separation of the RS and SR enantiomers of phenylpropanolamine (Solute #26) on a 25 cm column in PO mode as (A) ChiralPak IE column with a ACN/IPA (97:3, v/v) mobile phase with 0.1% BA and (B) Larihc CF6-P column with a ACN/MeOH (90:10, v/v) mobile phase with 0.3%TFA and 0.2%TEA additives. Flow rate: 2 mL/min; detection UV: 254 nm.

    Journal: Journal of Pharmaceutical Analysis

    Article Title: Screening primary racemic amines for enantioseparation by derivatized polysaccharide and cyclofructan columns

    doi: 10.1016/j.jpha.2016.07.003

    Figure Lengend Snippet: Separation of the RS and SR enantiomers of phenylpropanolamine (Solute #26) on a 25 cm column in PO mode as (A) ChiralPak IE column with a ACN/IPA (97:3, v/v) mobile phase with 0.1% BA and (B) Larihc CF6-P column with a ACN/MeOH (90:10, v/v) mobile phase with 0.3%TFA and 0.2%TEA additives. Flow rate: 2 mL/min; detection UV: 254 nm.

    Article Snippet: Acetonitrile (ACN), methanol (MeOH), ethanol (EtOH), n-heptane (hept), and isopropyl alcohol (IPA) of HPLC grade were obtained from VWR (Sugarland, Texas), and used as received.

    Techniques: Indirect Immunoperoxidase Assay, Flow Cytometry

    Representative comparison of analytical HPLC chromatograms from various RPIP conditions eluting persulfated N -cbz neomycin. Each chromatogram was generated from a 20 min. gradient increase in percent ACN, and the ending percent ACN was then maintained

    Journal: Carbohydrate research

    Article Title: Synthesis, separation, and characterization of amphiphilic sulfated oligosaccharides enabled by reversed-phase ion pairing LC and LC-MS methods

    doi: 10.1016/j.carres.2011.09.020

    Figure Lengend Snippet: Representative comparison of analytical HPLC chromatograms from various RPIP conditions eluting persulfated N -cbz neomycin. Each chromatogram was generated from a 20 min. gradient increase in percent ACN, and the ending percent ACN was then maintained

    Article Snippet: HPLC-grade acetonitrile (ACN) and triethylamine (TEA) were from Fisher Scientific (Hampton, NH, USA).

    Techniques: High Performance Liquid Chromatography, Generated

    HPLC chromatograms: ( a ) condition 1 with Agilent XDB-C18 at an isocratic mobile phase of acetonitrile (ACN):water (0.7% trifluoroacetic acid (TFA), 5 mM heptafluorobutyric acid (HFBA)) = 2:98; ( b ) condition 2 with YMC Triart-C8 at an isocratic mobile phase of ACN:water (0.7% TFA, 5 mM HFBA) = 2:98; ( c ) condition 3 with YMC Triart-C8 at an isocratic mobile phase of ACN:water (0.7% TFA, 5 mM HFBA) = 9:91; ( d ) after approximately 48 hours of repeated measurements with condition 3.

    Journal: Foods

    Article Title: New Analytical Approach for the Determination of Calcium Phosphate Dibasic and Tribasic in Processed Food by Comparison of Ion Chromatography with High-Performance Liquid Chromatography

    doi: 10.3390/foods9030248

    Figure Lengend Snippet: HPLC chromatograms: ( a ) condition 1 with Agilent XDB-C18 at an isocratic mobile phase of acetonitrile (ACN):water (0.7% trifluoroacetic acid (TFA), 5 mM heptafluorobutyric acid (HFBA)) = 2:98; ( b ) condition 2 with YMC Triart-C8 at an isocratic mobile phase of ACN:water (0.7% TFA, 5 mM HFBA) = 2:98; ( c ) condition 3 with YMC Triart-C8 at an isocratic mobile phase of ACN:water (0.7% TFA, 5 mM HFBA) = 9:91; ( d ) after approximately 48 hours of repeated measurements with condition 3.

    Article Snippet: Chemicals and Reagents Hexanes, HPLC grade water, and acetonitrile (ACN) were purchased from Honeywell Burdick and Jackson (Ulsan, Korea), and hydrochloric acid and calcium chloride anhydrous were obtained from Duksan Pure Chemical (Ansan, Korea).

    Techniques: High Performance Liquid Chromatography

    RP-HPLC analysis of PEGylated HM-3. Analysis was performed on a C18 column with water/ACN/TFA as eluent and a flow rate of 1 mL/min, and peaks were monitored at 220 nm. ( A ) ALD-mPEG 5k -HM-3 purity: 97.39%, T: 9.395 min; ( B ) ALD-mPEG 10k -HM-3 purity: 98.23%, T: 9.698 min; ( C ) SC-mPEG 10k -HM-3 purity: 97.02%, T: 9.883 min; ( D ) SC-mPEG 20k -HM-3 purity: 98.52%, T: 9.578 min.

    Journal: International Journal of Molecular Sciences

    Article Title: In Vivo Anti-Tumor Activity of Polypeptide HM-3 Modified by Different Polyethylene Glycols (PEG)

    doi: 10.3390/ijms12042650

    Figure Lengend Snippet: RP-HPLC analysis of PEGylated HM-3. Analysis was performed on a C18 column with water/ACN/TFA as eluent and a flow rate of 1 mL/min, and peaks were monitored at 220 nm. ( A ) ALD-mPEG 5k -HM-3 purity: 97.39%, T: 9.395 min; ( B ) ALD-mPEG 10k -HM-3 purity: 98.23%, T: 9.698 min; ( C ) SC-mPEG 10k -HM-3 purity: 97.02%, T: 9.883 min; ( D ) SC-mPEG 20k -HM-3 purity: 98.52%, T: 9.578 min.

    Article Snippet: Trifluoroacetate (TFA), acetonitrile (ACN), and sodium cyanoborohydride were purchased from TEDIA, ROE Scientific Inc., and Shanghai Darui Fine Chemicals Co. Ltd, respectively.

    Techniques: High Performance Liquid Chromatography, Flow Cytometry

    The UV spectrum and HPLC chromatogram of the oyster hydrolysate solution with different initial concentration and 5% final concentration of organic solvent for 40 min in the gradient model: (a) 0.1% TFA; (b) 0.1% TFA/ 0.8% ACN; (c) 0.1% TFA/1% ACN. TFA, trifluoroacetic acid; ACN, acetonitrile.

    Journal: BioMed Research International

    Article Title: Quantification of Multifunctional Dipeptide YA from Oyster Hydrolysate for Quality Control and Efficacy Evaluation

    doi: 10.1155/2018/8437379

    Figure Lengend Snippet: The UV spectrum and HPLC chromatogram of the oyster hydrolysate solution with different initial concentration and 5% final concentration of organic solvent for 40 min in the gradient model: (a) 0.1% TFA; (b) 0.1% TFA/ 0.8% ACN; (c) 0.1% TFA/1% ACN. TFA, trifluoroacetic acid; ACN, acetonitrile.

    Article Snippet: HPLC grade acetonitrile (ACN) and methanol (MeOH) were obtained from Burdick & Jackson (Muskegon, MI, USA).

    Techniques: High Performance Liquid Chromatography, Concentration Assay

    Detection of Cleaved Substrate Peptide by Mass Spectrometry A-B. 10 ng of recombinant AEP (rAEP) was incubated with 1 μg (0.65 mM) synthetic substrate peptide (hpvFAANDVSKvph) overnight at 37°C. Samples were dried down by vacuum centrifuge and resuspended in LB. 5 pmole of the substrate was loaded on to the liquid chromatography column and cleaved substrate was analysed by SRM MS (A) followed by an DDA workflow (B). (A) Three SRM transitions (b4-481.25 + , b5-552.29 + , b6-623.33 + ) were used to detect the cleaved substrate, sequenced as hpvFAAN (378.2 2+ precursor ion). The target peptide eluted at 32 min during the chromatographic gradient. (B) Product ion scans of precursor 378.2 2+ as analysed by DDA. C. Synthetic peptide sequenced as cleaved form of the substrate (hpvFAAN) was dissolved into HPLC grade water and seven different concentrations from 1 amole to 1 pmole were made in loading buffer (LB), containing 20 mM citric acid, 0.1% FA, 0.1% ACN. D. 10 amole, 100 amole, 1 fmole, 10 fmole, or 100 fmole of the substrate (hpvFAAN) peptide was spiked into normal plasma. Samples were precipitated using 2 volumes of ACN and dried down using vacuum centrifugation. Samples were resuspended in LB and analyzed by SRM MS. Error bars shown are +/−SEM (n = 3).

    Journal: Oncotarget

    Article Title: Development of a selected reaction monitoring mass spectrometry-based assay to detect asparaginyl endopeptidase activity in biological fluids

    doi: 10.18632/oncotarget.12224

    Figure Lengend Snippet: Detection of Cleaved Substrate Peptide by Mass Spectrometry A-B. 10 ng of recombinant AEP (rAEP) was incubated with 1 μg (0.65 mM) synthetic substrate peptide (hpvFAANDVSKvph) overnight at 37°C. Samples were dried down by vacuum centrifuge and resuspended in LB. 5 pmole of the substrate was loaded on to the liquid chromatography column and cleaved substrate was analysed by SRM MS (A) followed by an DDA workflow (B). (A) Three SRM transitions (b4-481.25 + , b5-552.29 + , b6-623.33 + ) were used to detect the cleaved substrate, sequenced as hpvFAAN (378.2 2+ precursor ion). The target peptide eluted at 32 min during the chromatographic gradient. (B) Product ion scans of precursor 378.2 2+ as analysed by DDA. C. Synthetic peptide sequenced as cleaved form of the substrate (hpvFAAN) was dissolved into HPLC grade water and seven different concentrations from 1 amole to 1 pmole were made in loading buffer (LB), containing 20 mM citric acid, 0.1% FA, 0.1% ACN. D. 10 amole, 100 amole, 1 fmole, 10 fmole, or 100 fmole of the substrate (hpvFAAN) peptide was spiked into normal plasma. Samples were precipitated using 2 volumes of ACN and dried down using vacuum centrifugation. Samples were resuspended in LB and analyzed by SRM MS. Error bars shown are +/−SEM (n = 3).

    Article Snippet: Chemicals Reagents were supplied as follows: HPLC grade water and 0.1% (w/v) formic acid with water, dithiothreitol (DTT) and 3-[(3-cholamidopropyl) dimethylammonio]-1-propanesulfonate (CHAPS) were from Sigma-Aldrich, St. Louis, MO; HPLC grade Acetonitrile (ACN) and hydrochloric acid (HCl) (VWR, Leicestershire, UK); Recombinant human AEP (rAEP), expressed in NS0 derived murine myeloma cell line, containing amino acids Ile18 to Tyr433 with an N-terminal 7 His tag, (R & D Systems, Abingdon, UK); AEP specific target peptides “hphFAANDVSKhph” (New England Peptides, Gardner, MA), “hpvFAANDVSKvph” and havFAANDVSKvah” including cleaved substrate “hpvFAAN” (JPT Innovative Peptide Solutions, Berlin, Germany); AnalaR grade Citric acid, di-sodium hydrogen phosphate (Na2 HPO4 ) and Ethylenediaminetetraacetic acid (EDTA) (DBH, UK) and Total Legumain DuoSet ELISA kit (R & D Systems).

    Techniques: Mass Spectrometry, Recombinant, Incubation, Liquid Chromatography, High Performance Liquid Chromatography, Centrifugation

    RP-HPLC separation on a capillary C18 column of the anion-exchange purified fraction containing the heteroconjugate. In (a) a gradient composed of buffer A: 5 mM ammonium acetate, 5% ACN/H 2 O and buffer B: 95% ACN/H 2 O was used. In (b) a gradient composed

    Journal:

    Article Title: APPLICATION OF FRACTIONAL MASS FOR THE IDENTIFICATION OF PEPTIDE:OLIGONUCLEOTIDE CROSS-LINKS BY MASS SPECTROMETRY

    doi: 10.1002/jms.1391

    Figure Lengend Snippet: RP-HPLC separation on a capillary C18 column of the anion-exchange purified fraction containing the heteroconjugate. In (a) a gradient composed of buffer A: 5 mM ammonium acetate, 5% ACN/H 2 O and buffer B: 95% ACN/H 2 O was used. In (b) a gradient composed

    Article Snippet: HPLC grade acetonitrile (ACN) and water were obtained from TEDIA (Fairfield, OH).

    Techniques: High Performance Liquid Chromatography, Purification