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    Structured Review

    Agilent technologies hplc ms ms
    Hplc Ms Ms, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 95/100, based on 64706 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/ms/Bio+LC/pmc13694530-111-4-5
    Average 95 stars, based on 64706 article reviews
    hplc ms ms - by Bioz Stars, 2026-11
    95/100 stars

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    Related Articles

    Solvent:

    Article Title: Production improvement of dalbavancin precursor A40926B0 in Nonomuraea gerenzanensis through strain reconstruction and fermentation optimization
    Article Snippet: 000 rpm for 10 min, and the supernatant was filtered through a 0.22 μm membrane filter. The filtrate was collected for HPLC analysis. HPLC analysis was performed using an Agilent 1260 Infinity system (Agilent Technologies, Santa Clara, CA, USA) equipped with an Agilent ZORBAX Eclipse Plus C18 column (5 μm, 4.6 × 250 mm). The mobile phase consisted of solvent A (ultrapure water containing 0.1% trifl

    High Performance Liquid Chromatography:

    Article Title: Production improvement of dalbavancin precursor A40926B0 in Nonomuraea gerenzanensis through strain reconstruction and fermentation optimization
    Article Snippet: 000 rpm for 10 min, and the supernatant was filtered through a 0.22 μm membrane filter. The filtrate was collected for HPLC analysis. HPLC analysis was performed using an Agilent 1260 Infinity system (Agilent Technologies, Santa Clara, CA, USA) equipped with an Agilent ZORBAX Eclipse Plus C18 column (5 μm, 4.6 × 250 mm). The mobile phase consisted of solvent A (ultrapure water containing 0.1% trifl

    Membrane:

    Article Title: Production improvement of dalbavancin precursor A40926B0 in Nonomuraea gerenzanensis through strain reconstruction and fermentation optimization
    Article Snippet: 000 rpm for 10 min, and the supernatant was filtered through a 0.22 μm membrane filter. The filtrate was collected for HPLC analysis. HPLC analysis was performed using an Agilent 1260 Infinity system (Agilent Technologies, Santa Clara, CA, USA) equipped with an Agilent ZORBAX Eclipse Plus C18 column (5 μm, 4.6 × 250 mm). The mobile phase consisted of solvent A (ultrapure water containing 0.1% trifl

    Gel Permeation Chromatography:

    Article Title: Production improvement of dalbavancin precursor A40926B0 in Nonomuraea gerenzanensis through strain reconstruction and fermentation optimization
    Article Snippet: 000 rpm for 10 min, and the supernatant was filtered through a 0.22 μm membrane filter. The filtrate was collected for HPLC analysis. HPLC analysis was performed using an Agilent 1260 Infinity system (Agilent Technologies, Santa Clara, CA, USA) equipped with an Agilent ZORBAX Eclipse Plus C18 column (5 μm, 4.6 × 250 mm). The mobile phase consisted of solvent A (ultrapure water containing 0.1% trifl

    Chromatography:

    Article Title: Production improvement of dalbavancin precursor A40926B0 in Nonomuraea gerenzanensis through strain reconstruction and fermentation optimization
    Article Snippet: 000 rpm for 10 min, and the supernatant was filtered through a 0.22 μm membrane filter. The filtrate was collected for HPLC analysis. HPLC analysis was performed using an Agilent 1260 Infinity system (Agilent Technologies, Santa Clara, CA, USA) equipped with an Agilent ZORBAX Eclipse Plus C18 column (5 μm, 4.6 × 250 mm). The mobile phase consisted of solvent A (ultrapure water containing 0.1% trifl

    Molecular Weight:

    Article Title: Production improvement of dalbavancin precursor A40926B0 in Nonomuraea gerenzanensis through strain reconstruction and fermentation optimization
    Article Snippet: 000 rpm for 10 min, and the supernatant was filtered through a 0.22 μm membrane filter. The filtrate was collected for HPLC analysis. HPLC analysis was performed using an Agilent 1260 Infinity system (Agilent Technologies, Santa Clara, CA, USA) equipped with an Agilent ZORBAX Eclipse Plus C18 column (5 μm, 4.6 × 250 mm). The mobile phase consisted of solvent A (ultrapure water containing 0.1% trifl

    Synthesized:

    Article Title: Production improvement of dalbavancin precursor A40926B0 in Nonomuraea gerenzanensis through strain reconstruction and fermentation optimization
    Article Snippet: 000 rpm for 10 min, and the supernatant was filtered through a 0.22 μm membrane filter. The filtrate was collected for HPLC analysis. HPLC analysis was performed using an Agilent 1260 Infinity system (Agilent Technologies, Santa Clara, CA, USA) equipped with an Agilent ZORBAX Eclipse Plus C18 column (5 μm, 4.6 × 250 mm). The mobile phase consisted of solvent A (ultrapure water containing 0.1% trifl

    GPC Assay:

    Article Title: Production improvement of dalbavancin precursor A40926B0 in Nonomuraea gerenzanensis through strain reconstruction and fermentation optimization
    Article Snippet: 000 rpm for 10 min, and the supernatant was filtered through a 0.22 μm membrane filter. The filtrate was collected for HPLC analysis. HPLC analysis was performed using an Agilent 1260 Infinity system (Agilent Technologies, Santa Clara, CA, USA) equipped with an Agilent ZORBAX Eclipse Plus C18 column (5 μm, 4.6 × 250 mm). The mobile phase consisted of solvent A (ultrapure water containing 0.1% trifl

    Targeted Proteomics:

    Article Title: Production improvement of dalbavancin precursor A40926B0 in Nonomuraea gerenzanensis through strain reconstruction and fermentation optimization
    Article Snippet: 000 rpm for 10 min, and the supernatant was filtered through a 0.22 μm membrane filter. The filtrate was collected for HPLC analysis. HPLC analysis was performed using an Agilent 1260 Infinity system (Agilent Technologies, Santa Clara, CA, USA) equipped with an Agilent ZORBAX Eclipse Plus C18 column (5 μm, 4.6 × 250 mm). The mobile phase consisted of solvent A (ultrapure water containing 0.1% trifl

    Mass Spectrometry:

    Article Title: Production improvement of dalbavancin precursor A40926B0 in Nonomuraea gerenzanensis through strain reconstruction and fermentation optimization
    Article Snippet: 000 rpm for 10 min, and the supernatant was filtered through a 0.22 μm membrane filter. The filtrate was collected for HPLC analysis. HPLC analysis was performed using an Agilent 1260 Infinity system (Agilent Technologies, Santa Clara, CA, USA) equipped with an Agilent ZORBAX Eclipse Plus C18 column (5 μm, 4.6 × 250 mm). The mobile phase consisted of solvent A (ultrapure water containing 0.1% trifl

    Injection:

    Article Title: Production improvement of dalbavancin precursor A40926B0 in Nonomuraea gerenzanensis through strain reconstruction and fermentation optimization
    Article Snippet: 000 rpm for 10 min, and the supernatant was filtered through a 0.22 μm membrane filter. The filtrate was collected for HPLC analysis. HPLC analysis was performed using an Agilent 1260 Infinity system (Agilent Technologies, Santa Clara, CA, USA) equipped with an Agilent ZORBAX Eclipse Plus C18 column (5 μm, 4.6 × 250 mm). The mobile phase consisted of solvent A (ultrapure water containing 0.1% trifl

    Liquid Chromatography:

    Article Title: Production improvement of dalbavancin precursor A40926B0 in Nonomuraea gerenzanensis through strain reconstruction and fermentation optimization
    Article Snippet: 000 rpm for 10 min, and the supernatant was filtered through a 0.22 μm membrane filter. The filtrate was collected for HPLC analysis. HPLC analysis was performed using an Agilent 1260 Infinity system (Agilent Technologies, Santa Clara, CA, USA) equipped with an Agilent ZORBAX Eclipse Plus C18 column (5 μm, 4.6 × 250 mm). The mobile phase consisted of solvent A (ultrapure water containing 0.1% trifl

    Liquid Chromatography with Mass Spectroscopy:

    Article Title: Production improvement of dalbavancin precursor A40926B0 in Nonomuraea gerenzanensis through strain reconstruction and fermentation optimization
    Article Snippet: 000 rpm for 10 min, and the supernatant was filtered through a 0.22 μm membrane filter. The filtrate was collected for HPLC analysis. HPLC analysis was performed using an Agilent 1260 Infinity system (Agilent Technologies, Santa Clara, CA, USA) equipped with an Agilent ZORBAX Eclipse Plus C18 column (5 μm, 4.6 × 250 mm). The mobile phase consisted of solvent A (ultrapure water containing 0.1% trifl

    Pore Size:

    Article Title: Production improvement of dalbavancin precursor A40926B0 in Nonomuraea gerenzanensis through strain reconstruction and fermentation optimization
    Article Snippet: 000 rpm for 10 min, and the supernatant was filtered through a 0.22 μm membrane filter. The filtrate was collected for HPLC analysis. HPLC analysis was performed using an Agilent 1260 Infinity system (Agilent Technologies, Santa Clara, CA, USA) equipped with an Agilent ZORBAX Eclipse Plus C18 column (5 μm, 4.6 × 250 mm). The mobile phase consisted of solvent A (ultrapure water containing 0.1% trifl

    Lyophilization:

    Article Title: Production improvement of dalbavancin precursor A40926B0 in Nonomuraea gerenzanensis through strain reconstruction and fermentation optimization
    Article Snippet: 000 rpm for 10 min, and the supernatant was filtered through a 0.22 μm membrane filter. The filtrate was collected for HPLC analysis. HPLC analysis was performed using an Agilent 1260 Infinity system (Agilent Technologies, Santa Clara, CA, USA) equipped with an Agilent ZORBAX Eclipse Plus C18 column (5 μm, 4.6 × 250 mm). The mobile phase consisted of solvent A (ultrapure water containing 0.1% trifl

    Incubation:

    Article Title: Production improvement of dalbavancin precursor A40926B0 in Nonomuraea gerenzanensis through strain reconstruction and fermentation optimization
    Article Snippet: 000 rpm for 10 min, and the supernatant was filtered through a 0.22 μm membrane filter. The filtrate was collected for HPLC analysis. HPLC analysis was performed using an Agilent 1260 Infinity system (Agilent Technologies, Santa Clara, CA, USA) equipped with an Agilent ZORBAX Eclipse Plus C18 column (5 μm, 4.6 × 250 mm). The mobile phase consisted of solvent A (ultrapure water containing 0.1% trifl

    Centrifugation:

    Article Title: Production improvement of dalbavancin precursor A40926B0 in Nonomuraea gerenzanensis through strain reconstruction and fermentation optimization
    Article Snippet: 000 rpm for 10 min, and the supernatant was filtered through a 0.22 μm membrane filter. The filtrate was collected for HPLC analysis. HPLC analysis was performed using an Agilent 1260 Infinity system (Agilent Technologies, Santa Clara, CA, USA) equipped with an Agilent ZORBAX Eclipse Plus C18 column (5 μm, 4.6 × 250 mm). The mobile phase consisted of solvent A (ultrapure water containing 0.1% trifl

    Formulation:

    Article Title: Production improvement of dalbavancin precursor A40926B0 in Nonomuraea gerenzanensis through strain reconstruction and fermentation optimization
    Article Snippet: 000 rpm for 10 min, and the supernatant was filtered through a 0.22 μm membrane filter. The filtrate was collected for HPLC analysis. HPLC analysis was performed using an Agilent 1260 Infinity system (Agilent Technologies, Santa Clara, CA, USA) equipped with an Agilent ZORBAX Eclipse Plus C18 column (5 μm, 4.6 × 250 mm). The mobile phase consisted of solvent A (ultrapure water containing 0.1% trifl



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    98
    Danaher Inc exion lc hplc ms system
    Reaction schemes <t>and</t> <t>LC-MS</t> analysis of Pp UGTs reactions with diosgenin and pennogenin . ( a ) Biosynthesis of trillin mediated by UGT91BP2 and UGT703R1–3 through transferring glucose from UDP-glucose to the C-3 OH position of diosgenin. ( b ) Extracted ion chromatograms (EICs) of the in vitro enzyme activity assays of recombinant UGT91BP2 and UGT703R1–3 with UDP-glucose and diosgenin showing the formation of trillin, as compared to the authentic trillin standard. Control is the empty expression vector. ( c ) MS spectra of the enzymatic reaction products in hydrogen and sodium ion adducts compared to the fragmentation pattern of the trillin standard. The product molecular ions [M + H] + and [M +Na] + and the feature fragment ion [M + H − Glc] + with m / z 415.32 are marked. Of note, additional peaks observed in the diosgenin EIC ( m / z 415.32) for UGT703R1–3 might correspond to substrate isomeric impurities, in-source adducts, or minor non-enzymatic by-products; these peaks, which arose from the extracted ion flow of the substrate m / z , did not co-elute with the product, trillin , and therefore did not affect the interpretation of the product formation. ( d ) Biosynthesis of pennogenin 3- O -glucoside mediated by the UGT703R1–3 through transferring glucose from UDP-glucose to the C-3 OH position of pennogenin. ( e ) EICs of the in vitro enzyme activity assays of recombinant UGT91BP2 and UGT703R1–3 with UDP-glucose and pennogenin showing the formation of pennogenin 3- O -glucoside, compared to the control empty expression vector. ( f ) MS/MS spectra ([M + H – Glc] + and [M + H – Glc − H 2 O] + ) of the enzymatic reaction products.
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    Reaction schemes and LC-MS analysis of Pp UGTs reactions with diosgenin and pennogenin . ( a ) Biosynthesis of trillin mediated by UGT91BP2 and UGT703R1–3 through transferring glucose from UDP-glucose to the C-3 OH position of diosgenin. ( b ) Extracted ion chromatograms (EICs) of the in vitro enzyme activity assays of recombinant UGT91BP2 and UGT703R1–3 with UDP-glucose and diosgenin showing the formation of trillin, as compared to the authentic trillin standard. Control is the empty expression vector. ( c ) MS spectra of the enzymatic reaction products in hydrogen and sodium ion adducts compared to the fragmentation pattern of the trillin standard. The product molecular ions [M + H] + and [M +Na] + and the feature fragment ion [M + H − Glc] + with m / z 415.32 are marked. Of note, additional peaks observed in the diosgenin EIC ( m / z 415.32) for UGT703R1–3 might correspond to substrate isomeric impurities, in-source adducts, or minor non-enzymatic by-products; these peaks, which arose from the extracted ion flow of the substrate m / z , did not co-elute with the product, trillin , and therefore did not affect the interpretation of the product formation. ( d ) Biosynthesis of pennogenin 3- O -glucoside mediated by the UGT703R1–3 through transferring glucose from UDP-glucose to the C-3 OH position of pennogenin. ( e ) EICs of the in vitro enzyme activity assays of recombinant UGT91BP2 and UGT703R1–3 with UDP-glucose and pennogenin showing the formation of pennogenin 3- O -glucoside, compared to the control empty expression vector. ( f ) MS/MS spectra ([M + H – Glc] + and [M + H – Glc − H 2 O] + ) of the enzymatic reaction products.

    Journal: Synthetic and Systems Biotechnology

    Article Title: Functional characterization of four glycosyltransferases for biosynthesis of steroidal saponins in medicinal plant Paris polyphylla

    doi: 10.1016/j.synbio.2026.04.002

    Figure Lengend Snippet: Reaction schemes and LC-MS analysis of Pp UGTs reactions with diosgenin and pennogenin . ( a ) Biosynthesis of trillin mediated by UGT91BP2 and UGT703R1–3 through transferring glucose from UDP-glucose to the C-3 OH position of diosgenin. ( b ) Extracted ion chromatograms (EICs) of the in vitro enzyme activity assays of recombinant UGT91BP2 and UGT703R1–3 with UDP-glucose and diosgenin showing the formation of trillin, as compared to the authentic trillin standard. Control is the empty expression vector. ( c ) MS spectra of the enzymatic reaction products in hydrogen and sodium ion adducts compared to the fragmentation pattern of the trillin standard. The product molecular ions [M + H] + and [M +Na] + and the feature fragment ion [M + H − Glc] + with m / z 415.32 are marked. Of note, additional peaks observed in the diosgenin EIC ( m / z 415.32) for UGT703R1–3 might correspond to substrate isomeric impurities, in-source adducts, or minor non-enzymatic by-products; these peaks, which arose from the extracted ion flow of the substrate m / z , did not co-elute with the product, trillin , and therefore did not affect the interpretation of the product formation. ( d ) Biosynthesis of pennogenin 3- O -glucoside mediated by the UGT703R1–3 through transferring glucose from UDP-glucose to the C-3 OH position of pennogenin. ( e ) EICs of the in vitro enzyme activity assays of recombinant UGT91BP2 and UGT703R1–3 with UDP-glucose and pennogenin showing the formation of pennogenin 3- O -glucoside, compared to the control empty expression vector. ( f ) MS/MS spectra ([M + H – Glc] + and [M + H – Glc − H 2 O] + ) of the enzymatic reaction products.

    Article Snippet: Liquid chromatography-mass spectrometry (LC-MS) was equipped with a YMC-Triart C18 column (250 mm × 4.6 mm, 5 μm), and the column temperature was set to 30 °C.

    Techniques: Liquid Chromatography with Mass Spectroscopy, Transferring, In Vitro, Activity Assay, Recombinant, Control, Expressing, Plasmid Preparation, Tandem Mass Spectroscopy