Structured Review

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.
Acetonitrile Acn, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 93/100, based on 28 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 93 stars, based on 28 article reviews
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Images

1) Product Images from "Kinin release from human kininogen by 10 aspartic proteases produced by pathogenic yeast Candida albicans"

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

Journal: BMC Microbiology

doi: 10.1186/s12866-015-0394-8

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.
Figure Legend 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.

Techniques Used: 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
Figure Legend 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

Techniques Used: 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.
Figure Legend 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.

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

2) Product Images from "Application of Hydrophilic Interaction Liquid Chromatography for the Quantification of Flavonoids in Genista tinctoria Extract"

Article Title: Application of Hydrophilic Interaction Liquid Chromatography for the Quantification of Flavonoids in Genista tinctoria Extract

Journal: Journal of Analytical Methods in Chemistry

doi: 10.1155/2016/3789348

The relationship between log⁡ k of flavonoids and log⁡ P . Mobile phase: 95% ACN/ammonium formate or 95% MeOH/ammonium formate. (a) Bare silica column; (b) ZIC column.
Figure Legend Snippet: The relationship between log⁡ k of flavonoids and log⁡ P . Mobile phase: 95% ACN/ammonium formate or 95% MeOH/ammonium formate. (a) Bare silica column; (b) ZIC column.

Techniques Used:

The retention factor as a function of ACN or MeOH content in the mobile phase. (a) Bare silica column; (b) ZIC column.
Figure Legend Snippet: The retention factor as a function of ACN or MeOH content in the mobile phase. (a) Bare silica column; (b) ZIC column.

Techniques Used:

3) Product Images from "Characterization of a novel α4/4-conotoxin, Qc1.2, from vermivorous Conus quercinus"

Article Title: Characterization of a novel α4/4-conotoxin, Qc1.2, from vermivorous Conus quercinus

Journal: Acta Biochimica et Biophysica Sinica

doi: 10.1093/abbs/gmp077

HPLC (A) and MS (B) analysis of the oxidative folding of Qc1.2 The major oxidation product, marked by the asterisk, was purified and used for further characterization. In (A), Qc1.2 was loaded onto a PepMap C 18 analytical column in 90% buffer A and eluted with a flow rate of 0.5 ml/min using the following gradient: 0–5 min, 10–15% buffer B; 5–29 min, 15–27% buffer B; 29–31 min, 27–100% buffer B. Buffer A, 0.1% TFA; buffer B, 0.1% TFA in 100% ACN. Absorbance was measured at 214 nm. MS measurement of the purified peptide was performed by ESI-MS on a Q-trap mass spectrometer gave an average mass 1552.0 (calculated mass 1551.8).
Figure Legend Snippet: HPLC (A) and MS (B) analysis of the oxidative folding of Qc1.2 The major oxidation product, marked by the asterisk, was purified and used for further characterization. In (A), Qc1.2 was loaded onto a PepMap C 18 analytical column in 90% buffer A and eluted with a flow rate of 0.5 ml/min using the following gradient: 0–5 min, 10–15% buffer B; 5–29 min, 15–27% buffer B; 29–31 min, 27–100% buffer B. Buffer A, 0.1% TFA; buffer B, 0.1% TFA in 100% ACN. Absorbance was measured at 214 nm. MS measurement of the purified peptide was performed by ESI-MS on a Q-trap mass spectrometer gave an average mass 1552.0 (calculated mass 1551.8).

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

4) Product Images from "The application of Box-Behnken-Design in the optimization of HPLC separation of fluoroquinolones"

Article Title: The application of Box-Behnken-Design in the optimization of HPLC separation of fluoroquinolones

Journal: Scientific Reports

doi: 10.1038/s41598-019-55761-z

The Pareto Diagram for six-factor analysis (A- ACN, B- MeOH, C- TEA, D- NaH 2 PO 4 , E- pH, F- flow).
Figure Legend Snippet: The Pareto Diagram for six-factor analysis (A- ACN, B- MeOH, C- TEA, D- NaH 2 PO 4 , E- pH, F- flow).

Techniques Used: Flow Cytometry

The Pareto Diagram for four-factor analysis (A-ACN, B-TEA, C-NaH 2 PO 4 , D-pH).
Figure Legend Snippet: The Pareto Diagram for four-factor analysis (A-ACN, B-TEA, C-NaH 2 PO 4 , D-pH).

Techniques Used:

Related Articles

High Performance Liquid Chromatography:

Article Title: Application of Hydrophilic Interaction Liquid Chromatography for the Quantification of Flavonoids in Genista tinctoria Extract
Article Snippet: .. Acetonitrile (ACN) and methanol (MeOH) were of HPLC grade from Merck (Darmstadt, Germany). ..

Article Title: Kinin release from human kininogen by 10 aspartic proteases produced by pathogenic yeast Candida albicans
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. .. After re-swelling on ice in the digestion buffer, which contained 12.5 ng/μL of sequence-grade modified trypsin (Promega, Madison, WI), 50 mM (NH4 )HCO3 , and 4 mM CaCl2 , the gel pieces were incubated overnight at 37°C.

Article Title: Characterization of a novel α4/4-conotoxin, Qc1.2, from vermivorous Conus quercinus
Article Snippet: .. Trifluoroacetic acid (TFA) and acetonitrile (ACN) for HPLC were from Merck (Darmstadt, Germany). ..

Staining:

Article Title: Kinin release from human kininogen by 10 aspartic proteases produced by pathogenic yeast Candida albicans
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. .. After re-swelling on ice in the digestion buffer, which contained 12.5 ng/μL of sequence-grade modified trypsin (Promega, Madison, WI), 50 mM (NH4 )HCO3 , and 4 mM CaCl2 , the gel pieces were incubated overnight at 37°C.

other:

Article Title: Systematic Evaluation of Chromatographic Parameters for Isoquinoline Alkaloids on XB-C18 Core-Shell Column Using Different Mobile Phase Compositions
Article Snippet: Optimization of Chromatographic Condition The chromatographic parameters were established in the range of 20–40% of acetonitrile (ACN) and 30–40% of methanol (MeOH) in water.

Liquid Chromatography:

Article Title: Proteomic Analyses Reveal New Insights on the Antimicrobial Mechanisms of Chitosan Biopolymers and Their Nanosized Particles against Escherichia coli
Article Snippet: .. Liquid Chromatography Electrospray Ionization Mass Spectrometry (LC-ESI-MS/MS) Desalted-peptide pellets were resuspended in 30 µL of 2% acetonitrile (ACN) (Merck, Darmstadt, Germany, DEU) and 0.1% formic acid (FA) (Sigma-Aldrich), and 5 µL of a replicate of each experimental condition were used to create a pooled sample for protein identification. .. The peptide mixture was then centrifuged at 14,000× g for 5 min, to remove the insoluble material, and the supernatant was collected in an adequate vial for LC injection.

Mass Spectrometry:

Article Title: Proteomic Analyses Reveal New Insights on the Antimicrobial Mechanisms of Chitosan Biopolymers and Their Nanosized Particles against Escherichia coli
Article Snippet: .. Liquid Chromatography Electrospray Ionization Mass Spectrometry (LC-ESI-MS/MS) Desalted-peptide pellets were resuspended in 30 µL of 2% acetonitrile (ACN) (Merck, Darmstadt, Germany, DEU) and 0.1% formic acid (FA) (Sigma-Aldrich), and 5 µL of a replicate of each experimental condition were used to create a pooled sample for protein identification. .. The peptide mixture was then centrifuged at 14,000× g for 5 min, to remove the insoluble material, and the supernatant was collected in an adequate vial for LC injection.

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    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.
    Acetonitrile Acn, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 93/100, based on 28 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/acetonitrile acn/product/Merck KGaA
    Average 93 stars, based on 28 article reviews
    Price from $9.99 to $1999.99
    acetonitrile acn - by Bioz Stars, 2020-07
    93/100 stars
      Buy from Supplier

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    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

    The relationship between log⁡ k of flavonoids and log⁡ P . Mobile phase: 95% ACN/ammonium formate or 95% MeOH/ammonium formate. (a) Bare silica column; (b) ZIC column.

    Journal: Journal of Analytical Methods in Chemistry

    Article Title: Application of Hydrophilic Interaction Liquid Chromatography for the Quantification of Flavonoids in Genista tinctoria Extract

    doi: 10.1155/2016/3789348

    Figure Lengend Snippet: The relationship between log⁡ k of flavonoids and log⁡ P . Mobile phase: 95% ACN/ammonium formate or 95% MeOH/ammonium formate. (a) Bare silica column; (b) ZIC column.

    Article Snippet: Acetonitrile (ACN) and methanol (MeOH) were of HPLC grade from Merck (Darmstadt, Germany).

    Techniques:

    The retention factor as a function of ACN or MeOH content in the mobile phase. (a) Bare silica column; (b) ZIC column.

    Journal: Journal of Analytical Methods in Chemistry

    Article Title: Application of Hydrophilic Interaction Liquid Chromatography for the Quantification of Flavonoids in Genista tinctoria Extract

    doi: 10.1155/2016/3789348

    Figure Lengend Snippet: The retention factor as a function of ACN or MeOH content in the mobile phase. (a) Bare silica column; (b) ZIC column.

    Article Snippet: Acetonitrile (ACN) and methanol (MeOH) were of HPLC grade from Merck (Darmstadt, Germany).

    Techniques:

    HPLC (A) and MS (B) analysis of the oxidative folding of Qc1.2 The major oxidation product, marked by the asterisk, was purified and used for further characterization. In (A), Qc1.2 was loaded onto a PepMap C 18 analytical column in 90% buffer A and eluted with a flow rate of 0.5 ml/min using the following gradient: 0–5 min, 10–15% buffer B; 5–29 min, 15–27% buffer B; 29–31 min, 27–100% buffer B. Buffer A, 0.1% TFA; buffer B, 0.1% TFA in 100% ACN. Absorbance was measured at 214 nm. MS measurement of the purified peptide was performed by ESI-MS on a Q-trap mass spectrometer gave an average mass 1552.0 (calculated mass 1551.8).

    Journal: Acta Biochimica et Biophysica Sinica

    Article Title: Characterization of a novel α4/4-conotoxin, Qc1.2, from vermivorous Conus quercinus

    doi: 10.1093/abbs/gmp077

    Figure Lengend Snippet: HPLC (A) and MS (B) analysis of the oxidative folding of Qc1.2 The major oxidation product, marked by the asterisk, was purified and used for further characterization. In (A), Qc1.2 was loaded onto a PepMap C 18 analytical column in 90% buffer A and eluted with a flow rate of 0.5 ml/min using the following gradient: 0–5 min, 10–15% buffer B; 5–29 min, 15–27% buffer B; 29–31 min, 27–100% buffer B. Buffer A, 0.1% TFA; buffer B, 0.1% TFA in 100% ACN. Absorbance was measured at 214 nm. MS measurement of the purified peptide was performed by ESI-MS on a Q-trap mass spectrometer gave an average mass 1552.0 (calculated mass 1551.8).

    Article Snippet: Trifluoroacetic acid (TFA) and acetonitrile (ACN) for HPLC were from Merck (Darmstadt, Germany).

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

    The Pareto Diagram for six-factor analysis (A- ACN, B- MeOH, C- TEA, D- NaH 2 PO 4 , E- pH, F- flow).

    Journal: Scientific Reports

    Article Title: The application of Box-Behnken-Design in the optimization of HPLC separation of fluoroquinolones

    doi: 10.1038/s41598-019-55761-z

    Figure Lengend Snippet: The Pareto Diagram for six-factor analysis (A- ACN, B- MeOH, C- TEA, D- NaH 2 PO 4 , E- pH, F- flow).

    Article Snippet: Reagents Acetonitrile (ACN), methanol (MeOH), triethylamine (TEA), dichloromethane (DCM) were purchased by Merck (Germany).

    Techniques: Flow Cytometry

    The Pareto Diagram for four-factor analysis (A-ACN, B-TEA, C-NaH 2 PO 4 , D-pH).

    Journal: Scientific Reports

    Article Title: The application of Box-Behnken-Design in the optimization of HPLC separation of fluoroquinolones

    doi: 10.1038/s41598-019-55761-z

    Figure Lengend Snippet: The Pareto Diagram for four-factor analysis (A-ACN, B-TEA, C-NaH 2 PO 4 , D-pH).

    Article Snippet: Reagents Acetonitrile (ACN), methanol (MeOH), triethylamine (TEA), dichloromethane (DCM) were purchased by Merck (Germany).

    Techniques: