Structured Review

Agilent technologies electrospray ionization esi mode
Detection of phosphorylated sphingosine analogs. (A) LC-HRMS verification of the identity of the clickable sphingosine analogs used and detection of a phosphorylation product of ω-N 3 -sphingosine catalyzed by SphK1 in vitro . Lipid extracts from incubation of 1-N 3 -sphingosine or ω-N 3 -sphingosine with SphK1 and ATP were chromatographically separated by HPLC and analyzed with a quadrupole-time-of-flight mass spectrometer (QTOF MS) operating in the positive <t>electrospray</t> ionization mode <t>(ESI+).</t> Chemical structures and mass spectra of ionized ω-N 3 -sphingosine (left), 1-N 3 -sphingosine (middle), and phosphorylated ω-N 3 -S1P (right) are shown. No phosphorylation product of 1-N 3 -sphingosine could be detected. The retention time (t R ) of each substance analyzed is given as inset (top left) in the respective mass spectrum. (B) Detection of ω-N 3 -sphingosine 1-phosphate in Chang cells by LC-MS/MS. Chang cells were incubated with either 1-N 3 -sphingosine or ω-N 3 -sphingosine (10 μM) for 17 h. Lipid extracts were analyzed by selected reaction monitoring (SRM) after positive electrospray ionization (ESI+). As expected, no phosphorylation product could be detected for 1-N 3 -sphingosine (not shown). On the other hand, both ω-N 3 -sphingosine (upper chromatogram) and ω-N 3 -S1P (lower chromatogram) were present in lipid extracts of Chang cells stimulated with ω-N 3 -sphingosine. Assuming similar MS/MS responses for precursor and phosphorylation product, a conversion of about 20% occurred under the given experimental conditions. Peaks are labeled with retention time. Structural formulas and MS/MS fragmentations monitored are given as insets. CID, collision-induced dissociation.
Electrospray Ionization Esi Mode, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 99/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "A Role of Sphingosine in the Intracellular Survival of Neisseria gonorrhoeae"

Article Title: A Role of Sphingosine in the Intracellular Survival of Neisseria gonorrhoeae

Journal: Frontiers in Cellular and Infection Microbiology

doi: 10.3389/fcimb.2020.00215

Detection of phosphorylated sphingosine analogs. (A) LC-HRMS verification of the identity of the clickable sphingosine analogs used and detection of a phosphorylation product of ω-N 3 -sphingosine catalyzed by SphK1 in vitro . Lipid extracts from incubation of 1-N 3 -sphingosine or ω-N 3 -sphingosine with SphK1 and ATP were chromatographically separated by HPLC and analyzed with a quadrupole-time-of-flight mass spectrometer (QTOF MS) operating in the positive electrospray ionization mode (ESI+). Chemical structures and mass spectra of ionized ω-N 3 -sphingosine (left), 1-N 3 -sphingosine (middle), and phosphorylated ω-N 3 -S1P (right) are shown. No phosphorylation product of 1-N 3 -sphingosine could be detected. The retention time (t R ) of each substance analyzed is given as inset (top left) in the respective mass spectrum. (B) Detection of ω-N 3 -sphingosine 1-phosphate in Chang cells by LC-MS/MS. Chang cells were incubated with either 1-N 3 -sphingosine or ω-N 3 -sphingosine (10 μM) for 17 h. Lipid extracts were analyzed by selected reaction monitoring (SRM) after positive electrospray ionization (ESI+). As expected, no phosphorylation product could be detected for 1-N 3 -sphingosine (not shown). On the other hand, both ω-N 3 -sphingosine (upper chromatogram) and ω-N 3 -S1P (lower chromatogram) were present in lipid extracts of Chang cells stimulated with ω-N 3 -sphingosine. Assuming similar MS/MS responses for precursor and phosphorylation product, a conversion of about 20% occurred under the given experimental conditions. Peaks are labeled with retention time. Structural formulas and MS/MS fragmentations monitored are given as insets. CID, collision-induced dissociation.
Figure Legend Snippet: Detection of phosphorylated sphingosine analogs. (A) LC-HRMS verification of the identity of the clickable sphingosine analogs used and detection of a phosphorylation product of ω-N 3 -sphingosine catalyzed by SphK1 in vitro . Lipid extracts from incubation of 1-N 3 -sphingosine or ω-N 3 -sphingosine with SphK1 and ATP were chromatographically separated by HPLC and analyzed with a quadrupole-time-of-flight mass spectrometer (QTOF MS) operating in the positive electrospray ionization mode (ESI+). Chemical structures and mass spectra of ionized ω-N 3 -sphingosine (left), 1-N 3 -sphingosine (middle), and phosphorylated ω-N 3 -S1P (right) are shown. No phosphorylation product of 1-N 3 -sphingosine could be detected. The retention time (t R ) of each substance analyzed is given as inset (top left) in the respective mass spectrum. (B) Detection of ω-N 3 -sphingosine 1-phosphate in Chang cells by LC-MS/MS. Chang cells were incubated with either 1-N 3 -sphingosine or ω-N 3 -sphingosine (10 μM) for 17 h. Lipid extracts were analyzed by selected reaction monitoring (SRM) after positive electrospray ionization (ESI+). As expected, no phosphorylation product could be detected for 1-N 3 -sphingosine (not shown). On the other hand, both ω-N 3 -sphingosine (upper chromatogram) and ω-N 3 -S1P (lower chromatogram) were present in lipid extracts of Chang cells stimulated with ω-N 3 -sphingosine. Assuming similar MS/MS responses for precursor and phosphorylation product, a conversion of about 20% occurred under the given experimental conditions. Peaks are labeled with retention time. Structural formulas and MS/MS fragmentations monitored are given as insets. CID, collision-induced dissociation.

Techniques Used: In Vitro, Incubation, High Performance Liquid Chromatography, Mass Spectrometry, Liquid Chromatography with Mass Spectroscopy, Tandem Mass Spectroscopy, Labeling

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    Agilent technologies electrospray ionization esi mode
    Detection of phosphorylated sphingosine analogs. (A) LC-HRMS verification of the identity of the clickable sphingosine analogs used and detection of a phosphorylation product of ω-N 3 -sphingosine catalyzed by SphK1 in vitro . Lipid extracts from incubation of 1-N 3 -sphingosine or ω-N 3 -sphingosine with SphK1 and ATP were chromatographically separated by HPLC and analyzed with a quadrupole-time-of-flight mass spectrometer (QTOF MS) operating in the positive <t>electrospray</t> ionization mode <t>(ESI+).</t> Chemical structures and mass spectra of ionized ω-N 3 -sphingosine (left), 1-N 3 -sphingosine (middle), and phosphorylated ω-N 3 -S1P (right) are shown. No phosphorylation product of 1-N 3 -sphingosine could be detected. The retention time (t R ) of each substance analyzed is given as inset (top left) in the respective mass spectrum. (B) Detection of ω-N 3 -sphingosine 1-phosphate in Chang cells by LC-MS/MS. Chang cells were incubated with either 1-N 3 -sphingosine or ω-N 3 -sphingosine (10 μM) for 17 h. Lipid extracts were analyzed by selected reaction monitoring (SRM) after positive electrospray ionization (ESI+). As expected, no phosphorylation product could be detected for 1-N 3 -sphingosine (not shown). On the other hand, both ω-N 3 -sphingosine (upper chromatogram) and ω-N 3 -S1P (lower chromatogram) were present in lipid extracts of Chang cells stimulated with ω-N 3 -sphingosine. Assuming similar MS/MS responses for precursor and phosphorylation product, a conversion of about 20% occurred under the given experimental conditions. Peaks are labeled with retention time. Structural formulas and MS/MS fragmentations monitored are given as insets. CID, collision-induced dissociation.
    Electrospray Ionization Esi Mode, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 89/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/electrospray ionization esi mode/product/Agilent technologies
    Average 89 stars, based on 12 article reviews
    Price from $9.99 to $1999.99
    electrospray ionization esi mode - by Bioz Stars, 2020-09
    89/100 stars
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    Detection of phosphorylated sphingosine analogs. (A) LC-HRMS verification of the identity of the clickable sphingosine analogs used and detection of a phosphorylation product of ω-N 3 -sphingosine catalyzed by SphK1 in vitro . Lipid extracts from incubation of 1-N 3 -sphingosine or ω-N 3 -sphingosine with SphK1 and ATP were chromatographically separated by HPLC and analyzed with a quadrupole-time-of-flight mass spectrometer (QTOF MS) operating in the positive electrospray ionization mode (ESI+). Chemical structures and mass spectra of ionized ω-N 3 -sphingosine (left), 1-N 3 -sphingosine (middle), and phosphorylated ω-N 3 -S1P (right) are shown. No phosphorylation product of 1-N 3 -sphingosine could be detected. The retention time (t R ) of each substance analyzed is given as inset (top left) in the respective mass spectrum. (B) Detection of ω-N 3 -sphingosine 1-phosphate in Chang cells by LC-MS/MS. Chang cells were incubated with either 1-N 3 -sphingosine or ω-N 3 -sphingosine (10 μM) for 17 h. Lipid extracts were analyzed by selected reaction monitoring (SRM) after positive electrospray ionization (ESI+). As expected, no phosphorylation product could be detected for 1-N 3 -sphingosine (not shown). On the other hand, both ω-N 3 -sphingosine (upper chromatogram) and ω-N 3 -S1P (lower chromatogram) were present in lipid extracts of Chang cells stimulated with ω-N 3 -sphingosine. Assuming similar MS/MS responses for precursor and phosphorylation product, a conversion of about 20% occurred under the given experimental conditions. Peaks are labeled with retention time. Structural formulas and MS/MS fragmentations monitored are given as insets. CID, collision-induced dissociation.

    Journal: Frontiers in Cellular and Infection Microbiology

    Article Title: A Role of Sphingosine in the Intracellular Survival of Neisseria gonorrhoeae

    doi: 10.3389/fcimb.2020.00215

    Figure Lengend Snippet: Detection of phosphorylated sphingosine analogs. (A) LC-HRMS verification of the identity of the clickable sphingosine analogs used and detection of a phosphorylation product of ω-N 3 -sphingosine catalyzed by SphK1 in vitro . Lipid extracts from incubation of 1-N 3 -sphingosine or ω-N 3 -sphingosine with SphK1 and ATP were chromatographically separated by HPLC and analyzed with a quadrupole-time-of-flight mass spectrometer (QTOF MS) operating in the positive electrospray ionization mode (ESI+). Chemical structures and mass spectra of ionized ω-N 3 -sphingosine (left), 1-N 3 -sphingosine (middle), and phosphorylated ω-N 3 -S1P (right) are shown. No phosphorylation product of 1-N 3 -sphingosine could be detected. The retention time (t R ) of each substance analyzed is given as inset (top left) in the respective mass spectrum. (B) Detection of ω-N 3 -sphingosine 1-phosphate in Chang cells by LC-MS/MS. Chang cells were incubated with either 1-N 3 -sphingosine or ω-N 3 -sphingosine (10 μM) for 17 h. Lipid extracts were analyzed by selected reaction monitoring (SRM) after positive electrospray ionization (ESI+). As expected, no phosphorylation product could be detected for 1-N 3 -sphingosine (not shown). On the other hand, both ω-N 3 -sphingosine (upper chromatogram) and ω-N 3 -S1P (lower chromatogram) were present in lipid extracts of Chang cells stimulated with ω-N 3 -sphingosine. Assuming similar MS/MS responses for precursor and phosphorylation product, a conversion of about 20% occurred under the given experimental conditions. Peaks are labeled with retention time. Structural formulas and MS/MS fragmentations monitored are given as insets. CID, collision-induced dissociation.

    Article Snippet: Briefly, chromatographic separations were performed with an Agilent 1260 Infinity HPLC coupled to an Agilent 6530 quadrupole-time-of-flight mass spectrometer (QTOF MS) operating in the positive electrospray ionization (ESI+) mode (Agilent Technologies, Waldbronn, Germany).

    Techniques: In Vitro, Incubation, High Performance Liquid Chromatography, Mass Spectrometry, Liquid Chromatography with Mass Spectroscopy, Tandem Mass Spectroscopy, Labeling