trifluoroacetic acid tfa Search Results


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  • 99
    Thermo Fisher trifluoroacetic acid
    Trifluoroacetic Acid, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 3914 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore trifluoroacetic acid
    Trifluoroacetic Acid, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 5667 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Waters Corporation trifluoroacetic acid tfa
    Trifluoroacetic Acid Tfa, supplied by Waters Corporation, used in various techniques. Bioz Stars score: 93/100, based on 1024 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Fisher Scientific trifluoroacetic acid tfa
    Synthesis of prodrug, a three step process including amino group protection of amino acid using phthaloylation; reaction of acetaminophen with N-protected amino acid and finally the deprotection (DCC=N,N-dicyclohexylcarbodiimide, DMAP=4-dimethylaminopyridine, <t>TFA=Trifluoroacetic</t> acid, DCM=Dichloromethane)
    Trifluoroacetic Acid Tfa, supplied by Fisher Scientific, used in various techniques. Bioz Stars score: 92/100, based on 355 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Waters Corporation trifluoroacetic acid
    Purification of a major cell wall protein by gel filtration and reverse-phase chromatographies. (A) Yeast cells ( mnn9 ) were cultured in YPAD medium with shaking for 30 h. The cell wall fraction was prepared and treated with SDS to remove noncovalently bound proteins. Cell wall proteins were solubilized with RPI. After centrifugation, 5 ml of the supernatant was applied to a Superdex 200 gel filtration column. The column was eluted isocratically with 10 mM Tris-HCl (pH 8.0) containing 150 mM NaCl and 0.05% sodium azide with a flow rate of 1 ml/min. The protein peak indicated by the bar was collected and lyophilized. (B) The collected peak in panel A was further purified by TSKgel Phenyl-5PW RP reverse-phase chromatography with a linear gradient of 5 to 80% acetonitrile in 0.05% <t>trifluoroacetic</t> acid. The protein peak indicated by the bar (gp260) was collected and lyophilized.
    Trifluoroacetic Acid, supplied by Waters Corporation, used in various techniques. Bioz Stars score: 92/100, based on 1261 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Merck KGaA trifluoroacetic acid tfa
    Purification of a major cell wall protein by gel filtration and reverse-phase chromatographies. (A) Yeast cells ( mnn9 ) were cultured in YPAD medium with shaking for 30 h. The cell wall fraction was prepared and treated with SDS to remove noncovalently bound proteins. Cell wall proteins were solubilized with RPI. After centrifugation, 5 ml of the supernatant was applied to a Superdex 200 gel filtration column. The column was eluted isocratically with 10 mM Tris-HCl (pH 8.0) containing 150 mM NaCl and 0.05% sodium azide with a flow rate of 1 ml/min. The protein peak indicated by the bar was collected and lyophilized. (B) The collected peak in panel A was further purified by TSKgel Phenyl-5PW RP reverse-phase chromatography with a linear gradient of 5 to 80% acetonitrile in 0.05% <t>trifluoroacetic</t> acid. The protein peak indicated by the bar (gp260) was collected and lyophilized.
    Trifluoroacetic Acid Tfa, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 93/100, based on 266 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Fisher Scientific trifluoroacetic acid
    Purification of a major cell wall protein by gel filtration and reverse-phase chromatographies. (A) Yeast cells ( mnn9 ) were cultured in YPAD medium with shaking for 30 h. The cell wall fraction was prepared and treated with SDS to remove noncovalently bound proteins. Cell wall proteins were solubilized with RPI. After centrifugation, 5 ml of the supernatant was applied to a Superdex 200 gel filtration column. The column was eluted isocratically with 10 mM Tris-HCl (pH 8.0) containing 150 mM NaCl and 0.05% sodium azide with a flow rate of 1 ml/min. The protein peak indicated by the bar was collected and lyophilized. (B) The collected peak in panel A was further purified by TSKgel Phenyl-5PW RP reverse-phase chromatography with a linear gradient of 5 to 80% acetonitrile in 0.05% <t>trifluoroacetic</t> acid. The protein peak indicated by the bar (gp260) was collected and lyophilized.
    Trifluoroacetic Acid, supplied by Fisher Scientific, used in various techniques. Bioz Stars score: 92/100, based on 364 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Merck KGaA trifluoroacetic acid
    Purification of a major cell wall protein by gel filtration and reverse-phase chromatographies. (A) Yeast cells ( mnn9 ) were cultured in YPAD medium with shaking for 30 h. The cell wall fraction was prepared and treated with SDS to remove noncovalently bound proteins. Cell wall proteins were solubilized with RPI. After centrifugation, 5 ml of the supernatant was applied to a Superdex 200 gel filtration column. The column was eluted isocratically with 10 mM Tris-HCl (pH 8.0) containing 150 mM NaCl and 0.05% sodium azide with a flow rate of 1 ml/min. The protein peak indicated by the bar was collected and lyophilized. (B) The collected peak in panel A was further purified by TSKgel Phenyl-5PW RP reverse-phase chromatography with a linear gradient of 5 to 80% acetonitrile in 0.05% <t>trifluoroacetic</t> acid. The protein peak indicated by the bar (gp260) was collected and lyophilized.
    Trifluoroacetic Acid, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 93/100, based on 424 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher tfa
    Purification of a major cell wall protein by gel filtration and reverse-phase chromatographies. (A) Yeast cells ( mnn9 ) were cultured in YPAD medium with shaking for 30 h. The cell wall fraction was prepared and treated with SDS to remove noncovalently bound proteins. Cell wall proteins were solubilized with RPI. After centrifugation, 5 ml of the supernatant was applied to a Superdex 200 gel filtration column. The column was eluted isocratically with 10 mM Tris-HCl (pH 8.0) containing 150 mM NaCl and 0.05% sodium azide with a flow rate of 1 ml/min. The protein peak indicated by the bar was collected and lyophilized. (B) The collected peak in panel A was further purified by TSKgel Phenyl-5PW RP reverse-phase chromatography with a linear gradient of 5 to 80% acetonitrile in 0.05% <t>trifluoroacetic</t> acid. The protein peak indicated by the bar (gp260) was collected and lyophilized.
    Tfa, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 818 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Agilent technologies trifluoroacetic acid
    Purification of a major cell wall protein by gel filtration and reverse-phase chromatographies. (A) Yeast cells ( mnn9 ) were cultured in YPAD medium with shaking for 30 h. The cell wall fraction was prepared and treated with SDS to remove noncovalently bound proteins. Cell wall proteins were solubilized with RPI. After centrifugation, 5 ml of the supernatant was applied to a Superdex 200 gel filtration column. The column was eluted isocratically with 10 mM Tris-HCl (pH 8.0) containing 150 mM NaCl and 0.05% sodium azide with a flow rate of 1 ml/min. The protein peak indicated by the bar was collected and lyophilized. (B) The collected peak in panel A was further purified by TSKgel Phenyl-5PW RP reverse-phase chromatography with a linear gradient of 5 to 80% acetonitrile in 0.05% <t>trifluoroacetic</t> acid. The protein peak indicated by the bar (gp260) was collected and lyophilized.
    Trifluoroacetic Acid, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 93/100, based on 641 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Avantor trifluoroacetic acid
    Reversed-phase FPLC of fraction VIIIB resulting from the Ts venom fractionation procedure. The fraction VIIIB was submitted to a reversed-phase chromatography on a C18 column (4.6 mm × 250 mm, 5 μm particles) equilibrated with 0.1% ( v / v ) of <t>trifluoroacetic</t> acid (TFA). Adsorbed proteins were eluted using a concentration gradient from 0% to 100% of solution B (80% acetonitrile in 0.1% TFA), represented by the dotted line. Flow: 0.8 mL/min. Absorbance was monitored at 214 nm, at 25 °C.
    Trifluoroacetic Acid, supplied by Avantor, used in various techniques. Bioz Stars score: 93/100, based on 228 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Merck & Co trifluoroacetic acid tfa
    Reversed-phase FPLC of fraction VIIIB resulting from the Ts venom fractionation procedure. The fraction VIIIB was submitted to a reversed-phase chromatography on a C18 column (4.6 mm × 250 mm, 5 μm particles) equilibrated with 0.1% ( v / v ) of <t>trifluoroacetic</t> acid (TFA). Adsorbed proteins were eluted using a concentration gradient from 0% to 100% of solution B (80% acetonitrile in 0.1% TFA), represented by the dotted line. Flow: 0.8 mL/min. Absorbance was monitored at 214 nm, at 25 °C.
    Trifluoroacetic Acid Tfa, supplied by Merck & Co, used in various techniques. Bioz Stars score: 93/100, based on 150 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Merck & Co trifluoroacetic acid
    Reversed-phase FPLC of fraction VIIIB resulting from the Ts venom fractionation procedure. The fraction VIIIB was submitted to a reversed-phase chromatography on a C18 column (4.6 mm × 250 mm, 5 μm particles) equilibrated with 0.1% ( v / v ) of <t>trifluoroacetic</t> acid (TFA). Adsorbed proteins were eluted using a concentration gradient from 0% to 100% of solution B (80% acetonitrile in 0.1% TFA), represented by the dotted line. Flow: 0.8 mL/min. Absorbance was monitored at 214 nm, at 25 °C.
    Trifluoroacetic Acid, supplied by Merck & Co, used in various techniques. Bioz Stars score: 92/100, based on 154 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    FUJIFILM trifluoroacetic acid tfa
    Reversed-phase FPLC of fraction VIIIB resulting from the Ts venom fractionation procedure. The fraction VIIIB was submitted to a reversed-phase chromatography on a C18 column (4.6 mm × 250 mm, 5 μm particles) equilibrated with 0.1% ( v / v ) of <t>trifluoroacetic</t> acid (TFA). Adsorbed proteins were eluted using a concentration gradient from 0% to 100% of solution B (80% acetonitrile in 0.1% TFA), represented by the dotted line. Flow: 0.8 mL/min. Absorbance was monitored at 214 nm, at 25 °C.
    Trifluoroacetic Acid Tfa, supplied by FUJIFILM, used in various techniques. Bioz Stars score: 93/100, based on 115 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Avantor trifluoroacetic acid tfa
    Reversed-phase FPLC of fraction VIIIB resulting from the Ts venom fractionation procedure. The fraction VIIIB was submitted to a reversed-phase chromatography on a C18 column (4.6 mm × 250 mm, 5 μm particles) equilibrated with 0.1% ( v / v ) of <t>trifluoroacetic</t> acid (TFA). Adsorbed proteins were eluted using a concentration gradient from 0% to 100% of solution B (80% acetonitrile in 0.1% TFA), represented by the dotted line. Flow: 0.8 mL/min. Absorbance was monitored at 214 nm, at 25 °C.
    Trifluoroacetic Acid Tfa, supplied by Avantor, used in various techniques. Bioz Stars score: 93/100, based on 167 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Biosolve trifluoroacetic acid tfa
    Reversed-phase FPLC of fraction VIIIB resulting from the Ts venom fractionation procedure. The fraction VIIIB was submitted to a reversed-phase chromatography on a C18 column (4.6 mm × 250 mm, 5 μm particles) equilibrated with 0.1% ( v / v ) of <t>trifluoroacetic</t> acid (TFA). Adsorbed proteins were eluted using a concentration gradient from 0% to 100% of solution B (80% acetonitrile in 0.1% TFA), represented by the dotted line. Flow: 0.8 mL/min. Absorbance was monitored at 214 nm, at 25 °C.
    Trifluoroacetic Acid Tfa, supplied by Biosolve, used in various techniques. Bioz Stars score: 93/100, based on 93 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    FUJIFILM trifluoroacetic acid
    HPLC chromatograms of (A) coumarin (10 mg/mL, standard) and (B) TJ-125. Chromatographic peaks were detected at a wavelength of 273 nm. The mobile phase consisted of water, acetonitrile and <t>trifluoroacetic</t> acid (750:250:0.5, v/v/v). The flow rate of the mobile phase was 0.5 ml/min. The injection volume was 10 μL. The column temperature was set at 40°C. The retention time of coumarin was 13.7 min.
    Trifluoroacetic Acid, supplied by FUJIFILM, used in various techniques. Bioz Stars score: 93/100, based on 159 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher trifluoroacetic acid salt
    HPLC chromatograms of (A) coumarin (10 mg/mL, standard) and (B) TJ-125. Chromatographic peaks were detected at a wavelength of 273 nm. The mobile phase consisted of water, acetonitrile and <t>trifluoroacetic</t> acid (750:250:0.5, v/v/v). The flow rate of the mobile phase was 0.5 ml/min. The injection volume was 10 μL. The column temperature was set at 40°C. The retention time of coumarin was 13.7 min.
    Trifluoroacetic Acid Salt, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 228 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Tedia trifluoroacetic acid
    HPLC chromatograms of (A) coumarin (10 mg/mL, standard) and (B) TJ-125. Chromatographic peaks were detected at a wavelength of 273 nm. The mobile phase consisted of water, acetonitrile and <t>trifluoroacetic</t> acid (750:250:0.5, v/v/v). The flow rate of the mobile phase was 0.5 ml/min. The injection volume was 10 μL. The column temperature was set at 40°C. The retention time of coumarin was 13.7 min.
    Trifluoroacetic Acid, supplied by Tedia, used in various techniques. Bioz Stars score: 92/100, based on 77 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Agilent technologies trifluoroacetic acid tfa
    Xylanase-dependent oligosaccharide profiles reveal differences in the digestibility of seed coat mucilage from different Plantago species. Extruded seed mucilage was subjected to GH10 xylanase digestion. (A) untreated mucilage. (B) mucilage samples pre-treated with <t>trifluoroacetic</t> acid <t>(TFA).</t> Only P. cunninghamii , P. debilis , and P. lanceolata showed cleaved products (oligosaccharides) when incubated with the GH10 xylanase without TFA pre-treatment. All mucilage samples produced different oligosaccharide maps when pre-treated with TFA. The chromatograms have been off-set to aid interpretation. Elution times for xylose and xylobiose 2.5 min and 3.25 min, respectively.
    Trifluoroacetic Acid Tfa, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 93/100, based on 191 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Biosolve trifluoroacetic acid
    Xylanase-dependent oligosaccharide profiles reveal differences in the digestibility of seed coat mucilage from different Plantago species. Extruded seed mucilage was subjected to GH10 xylanase digestion. (A) untreated mucilage. (B) mucilage samples pre-treated with <t>trifluoroacetic</t> acid <t>(TFA).</t> Only P. cunninghamii , P. debilis , and P. lanceolata showed cleaved products (oligosaccharides) when incubated with the GH10 xylanase without TFA pre-treatment. All mucilage samples produced different oligosaccharide maps when pre-treated with TFA. The chromatograms have been off-set to aid interpretation. Elution times for xylose and xylobiose 2.5 min and 3.25 min, respectively.
    Trifluoroacetic Acid, supplied by Biosolve, used in various techniques. Bioz Stars score: 92/100, based on 91 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Synthesis of prodrug, a three step process including amino group protection of amino acid using phthaloylation; reaction of acetaminophen with N-protected amino acid and finally the deprotection (DCC=N,N-dicyclohexylcarbodiimide, DMAP=4-dimethylaminopyridine, TFA=Trifluoroacetic acid, DCM=Dichloromethane)

    Journal: Indian Journal of Pharmacology

    Article Title: Pharmacological screening of glycine amino acid prodrug of acetaminophen

    doi: 10.4103/0253-7613.153431

    Figure Lengend Snippet: Synthesis of prodrug, a three step process including amino group protection of amino acid using phthaloylation; reaction of acetaminophen with N-protected amino acid and finally the deprotection (DCC=N,N-dicyclohexylcarbodiimide, DMAP=4-dimethylaminopyridine, TFA=Trifluoroacetic acid, DCM=Dichloromethane)

    Article Snippet: All the chemicals used were purchased from Loba Chemie except for trifluoroacetic acid (TFA) and dichloromethane (DCM), which were purchased from Fisher scientific.

    Techniques: Droplet Countercurrent Chromatography

    Purification of a major cell wall protein by gel filtration and reverse-phase chromatographies. (A) Yeast cells ( mnn9 ) were cultured in YPAD medium with shaking for 30 h. The cell wall fraction was prepared and treated with SDS to remove noncovalently bound proteins. Cell wall proteins were solubilized with RPI. After centrifugation, 5 ml of the supernatant was applied to a Superdex 200 gel filtration column. The column was eluted isocratically with 10 mM Tris-HCl (pH 8.0) containing 150 mM NaCl and 0.05% sodium azide with a flow rate of 1 ml/min. The protein peak indicated by the bar was collected and lyophilized. (B) The collected peak in panel A was further purified by TSKgel Phenyl-5PW RP reverse-phase chromatography with a linear gradient of 5 to 80% acetonitrile in 0.05% trifluoroacetic acid. The protein peak indicated by the bar (gp260) was collected and lyophilized.

    Journal: Journal of Bacteriology

    Article Title: Sed1p Is a Major Cell Wall Protein of Saccharomyces cerevisiae in the Stationary Phase and Is Involved in Lytic Enzyme Resistance

    doi:

    Figure Lengend Snippet: Purification of a major cell wall protein by gel filtration and reverse-phase chromatographies. (A) Yeast cells ( mnn9 ) were cultured in YPAD medium with shaking for 30 h. The cell wall fraction was prepared and treated with SDS to remove noncovalently bound proteins. Cell wall proteins were solubilized with RPI. After centrifugation, 5 ml of the supernatant was applied to a Superdex 200 gel filtration column. The column was eluted isocratically with 10 mM Tris-HCl (pH 8.0) containing 150 mM NaCl and 0.05% sodium azide with a flow rate of 1 ml/min. The protein peak indicated by the bar was collected and lyophilized. (B) The collected peak in panel A was further purified by TSKgel Phenyl-5PW RP reverse-phase chromatography with a linear gradient of 5 to 80% acetonitrile in 0.05% trifluoroacetic acid. The protein peak indicated by the bar (gp260) was collected and lyophilized.

    Article Snippet: Purified protein (2 nmol) was dissolved in 10 mM Tris-HCl (pH 9.0) containing 10 pmol of Achromobacter protease I (Takara, Kyoto, Japan), and incubated at 37°C for 15 h. After the reaction was stopped by adding 0.1% trifluoroacetic acid, the produced peptides were subjected to reverse-phase chromatography (μBondasphere C18 100 Å; Waters, Milford, Mass.) and eluted with a linear gradient of 5 to 40% acetonitrile in 0.1% trifluoroacetic acid.

    Techniques: Purification, Filtration, Cell Culture, Centrifugation, Flow Cytometry, Reversed-phase Chromatography

    Reverse-phase chromatography of hydrolysates of gp260 with Achromobacter protease I. After gp260 and Achromobacter protease I (200:1 by molar ratio) were incubated at 37°C for 15 h, the hydrolysate was fractionated with a μBondasphere C 18 reverse-phase chromatography column with a linear gradient of 5 to 40% acetonitrile in 0.1% trifluoroacetic acid. The numbered peaks were collected, and their amino acid sequences were determined.

    Journal: Journal of Bacteriology

    Article Title: Sed1p Is a Major Cell Wall Protein of Saccharomyces cerevisiae in the Stationary Phase and Is Involved in Lytic Enzyme Resistance

    doi:

    Figure Lengend Snippet: Reverse-phase chromatography of hydrolysates of gp260 with Achromobacter protease I. After gp260 and Achromobacter protease I (200:1 by molar ratio) were incubated at 37°C for 15 h, the hydrolysate was fractionated with a μBondasphere C 18 reverse-phase chromatography column with a linear gradient of 5 to 40% acetonitrile in 0.1% trifluoroacetic acid. The numbered peaks were collected, and their amino acid sequences were determined.

    Article Snippet: Purified protein (2 nmol) was dissolved in 10 mM Tris-HCl (pH 9.0) containing 10 pmol of Achromobacter protease I (Takara, Kyoto, Japan), and incubated at 37°C for 15 h. After the reaction was stopped by adding 0.1% trifluoroacetic acid, the produced peptides were subjected to reverse-phase chromatography (μBondasphere C18 100 Å; Waters, Milford, Mass.) and eluted with a linear gradient of 5 to 40% acetonitrile in 0.1% trifluoroacetic acid.

    Techniques: Reversed-phase Chromatography, Incubation

    Reversed-phase FPLC of fraction VIIIB resulting from the Ts venom fractionation procedure. The fraction VIIIB was submitted to a reversed-phase chromatography on a C18 column (4.6 mm × 250 mm, 5 μm particles) equilibrated with 0.1% ( v / v ) of trifluoroacetic acid (TFA). Adsorbed proteins were eluted using a concentration gradient from 0% to 100% of solution B (80% acetonitrile in 0.1% TFA), represented by the dotted line. Flow: 0.8 mL/min. Absorbance was monitored at 214 nm, at 25 °C.

    Journal: Toxins

    Article Title: Revealing the Function and the Structural Model of Ts4: Insights into the “Non-Toxic” Toxin from Tityus serrulatus Venom

    doi: 10.3390/toxins7072534

    Figure Lengend Snippet: Reversed-phase FPLC of fraction VIIIB resulting from the Ts venom fractionation procedure. The fraction VIIIB was submitted to a reversed-phase chromatography on a C18 column (4.6 mm × 250 mm, 5 μm particles) equilibrated with 0.1% ( v / v ) of trifluoroacetic acid (TFA). Adsorbed proteins were eluted using a concentration gradient from 0% to 100% of solution B (80% acetonitrile in 0.1% TFA), represented by the dotted line. Flow: 0.8 mL/min. Absorbance was monitored at 214 nm, at 25 °C.

    Article Snippet: RP-FPLC of the fraction VIIIB was performed in an Äkta Purifier UPC-10 system (GE Healthcare, Uppsala, Sweden), using a 4.6 mm × 250.0 mm C18 column (Shimadzu Corp., Kyoto, Kansai, Japan) equilibrated with 0.1% (v /v ) trifluoroacetic acid (TFA, Avantor Performance Materials Inc., Center Valley, PA, USA) at a flow rate of 0.8 mL/min.

    Techniques: Fast Protein Liquid Chromatography, Fractionation, Reversed-phase Chromatography, Concentration Assay, Flow Cytometry

    HPLC chromatograms of (A) coumarin (10 mg/mL, standard) and (B) TJ-125. Chromatographic peaks were detected at a wavelength of 273 nm. The mobile phase consisted of water, acetonitrile and trifluoroacetic acid (750:250:0.5, v/v/v). The flow rate of the mobile phase was 0.5 ml/min. The injection volume was 10 μL. The column temperature was set at 40°C. The retention time of coumarin was 13.7 min.

    Journal: Frontiers in Pharmacology

    Article Title: The Relation between Hepatotoxicity and the Total Coumarin Intake from Traditional Japanese Medicines Containing Cinnamon Bark

    doi: 10.3389/fphar.2016.00174

    Figure Lengend Snippet: HPLC chromatograms of (A) coumarin (10 mg/mL, standard) and (B) TJ-125. Chromatographic peaks were detected at a wavelength of 273 nm. The mobile phase consisted of water, acetonitrile and trifluoroacetic acid (750:250:0.5, v/v/v). The flow rate of the mobile phase was 0.5 ml/min. The injection volume was 10 μL. The column temperature was set at 40°C. The retention time of coumarin was 13.7 min.

    Article Snippet: Materials Coumarin, acetonitrile (HPLC grade), methanol (HPLC grade), and trifluoroacetic acid were purchased from Wako Pure Chemical Industries (Osaka, Japan).

    Techniques: High Performance Liquid Chromatography, Flow Cytometry, Injection

    Xylanase-dependent oligosaccharide profiles reveal differences in the digestibility of seed coat mucilage from different Plantago species. Extruded seed mucilage was subjected to GH10 xylanase digestion. (A) untreated mucilage. (B) mucilage samples pre-treated with trifluoroacetic acid (TFA). Only P. cunninghamii , P. debilis , and P. lanceolata showed cleaved products (oligosaccharides) when incubated with the GH10 xylanase without TFA pre-treatment. All mucilage samples produced different oligosaccharide maps when pre-treated with TFA. The chromatograms have been off-set to aid interpretation. Elution times for xylose and xylobiose 2.5 min and 3.25 min, respectively.

    Journal: Journal of Experimental Botany

    Article Title: Differences in glycosyltransferase family 61 accompany variation in seed coat mucilage composition in Plantago spp.

    doi: 10.1093/jxb/erw424

    Figure Lengend Snippet: Xylanase-dependent oligosaccharide profiles reveal differences in the digestibility of seed coat mucilage from different Plantago species. Extruded seed mucilage was subjected to GH10 xylanase digestion. (A) untreated mucilage. (B) mucilage samples pre-treated with trifluoroacetic acid (TFA). Only P. cunninghamii , P. debilis , and P. lanceolata showed cleaved products (oligosaccharides) when incubated with the GH10 xylanase without TFA pre-treatment. All mucilage samples produced different oligosaccharide maps when pre-treated with TFA. The chromatograms have been off-set to aid interpretation. Elution times for xylose and xylobiose 2.5 min and 3.25 min, respectively.

    Article Snippet: Pre-treatment Ground Plantago seed mucilage was treated with 0.1 M trifluoroacetic acid (TFA) (Agilent Technologies, USA, G2007A) at 85 °C for 60 min with gentle shaking and precipitated with a series of 70% ethanol washes.

    Techniques: Incubation, Produced