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Agilent technologies reverse phase hplc
In vitro drug release behaviors of LPNs and the solution depicted as the cumulative <t>RPV</t> release (%) vs time. Notes: Data represent mean ± SD, N=3. Release of RPV from the LPNs was studied following the dialysis bag method. The bags were placed in a glass beaker containing 0.2 L of PBS (pH 7.4) at 37.0°C±0.5°C and stirred at 100 rpm. At pre-set time intervals, 1 mL of the medium was collected and analyzed for RPV content by <t>HPLC.</t> Abbreviations: RPV, ropivacaine; LPNs, lipid-polymer hybrid nanoparticles.
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1) Product Images from "An efficient and long-acting local anesthetic: ropivacaine-loaded lipid-polymer hybrid nanoparticles for the control of pain"

Article Title: An efficient and long-acting local anesthetic: ropivacaine-loaded lipid-polymer hybrid nanoparticles for the control of pain

Journal: International Journal of Nanomedicine

doi: 10.2147/IJN.S190164

In vitro drug release behaviors of LPNs and the solution depicted as the cumulative RPV release (%) vs time. Notes: Data represent mean ± SD, N=3. Release of RPV from the LPNs was studied following the dialysis bag method. The bags were placed in a glass beaker containing 0.2 L of PBS (pH 7.4) at 37.0°C±0.5°C and stirred at 100 rpm. At pre-set time intervals, 1 mL of the medium was collected and analyzed for RPV content by HPLC. Abbreviations: RPV, ropivacaine; LPNs, lipid-polymer hybrid nanoparticles.
Figure Legend Snippet: In vitro drug release behaviors of LPNs and the solution depicted as the cumulative RPV release (%) vs time. Notes: Data represent mean ± SD, N=3. Release of RPV from the LPNs was studied following the dialysis bag method. The bags were placed in a glass beaker containing 0.2 L of PBS (pH 7.4) at 37.0°C±0.5°C and stirred at 100 rpm. At pre-set time intervals, 1 mL of the medium was collected and analyzed for RPV content by HPLC. Abbreviations: RPV, ropivacaine; LPNs, lipid-polymer hybrid nanoparticles.

Techniques Used: In Vitro, High Performance Liquid Chromatography

2) Product Images from "Detection of Antioxidant Phytochemicals Isolated from Camellia japonica Seeds Using HPLC and EPR Imaging"

Article Title: Detection of Antioxidant Phytochemicals Isolated from Camellia japonica Seeds Using HPLC and EPR Imaging

Journal: Antioxidants

doi: 10.3390/antiox9060493

HPLC chromatograms of ( A ) the methanolic extract of C. japonica seed coats and ( B ) mixed catechin and related compounds were used as standards. The peaks are ( a ) gallic acid, ( b ) gallocatechin, ( c ) epigallocatechin, ( d ) caffeine, ( e ) catechin, ( f ) epicatechin, ( g ) epigallocatechin gallate, ( h ) gallocatechin gallate and ( i ) epicatechin gallate.
Figure Legend Snippet: HPLC chromatograms of ( A ) the methanolic extract of C. japonica seed coats and ( B ) mixed catechin and related compounds were used as standards. The peaks are ( a ) gallic acid, ( b ) gallocatechin, ( c ) epigallocatechin, ( d ) caffeine, ( e ) catechin, ( f ) epicatechin, ( g ) epigallocatechin gallate, ( h ) gallocatechin gallate and ( i ) epicatechin gallate.

Techniques Used: High Performance Liquid Chromatography

3) Product Images from "Detection of Antioxidant Phytochemicals Isolated from Camellia japonica Seeds Using HPLC and EPR Imaging"

Article Title: Detection of Antioxidant Phytochemicals Isolated from Camellia japonica Seeds Using HPLC and EPR Imaging

Journal: Antioxidants

doi: 10.3390/antiox9060493

HPLC chromatograms of hexane extract of ( A ) hexane extract of C. japonica seed coats and ( B ) mixed tocotrienols and tocopherols standards. The peaks are ( a ): δ-tocotrienol; ( b ): β-tocotrienol; ( c ): γ-tocotrienol; ( d ): α-tocotrienol; ( e ): δ-tocopherol; ( f ): β-tocopherol; ( g ): γ-tocopherol; and ( h ): α-tocopherol.
Figure Legend Snippet: HPLC chromatograms of hexane extract of ( A ) hexane extract of C. japonica seed coats and ( B ) mixed tocotrienols and tocopherols standards. The peaks are ( a ): δ-tocotrienol; ( b ): β-tocotrienol; ( c ): γ-tocotrienol; ( d ): α-tocotrienol; ( e ): δ-tocopherol; ( f ): β-tocopherol; ( g ): γ-tocopherol; and ( h ): α-tocopherol.

Techniques Used: High Performance Liquid Chromatography

4) Product Images from "The molecular basis for selective inhibition of unconventional mRNA splicing by an IRE1-binding small molecule"

Article Title: The molecular basis for selective inhibition of unconventional mRNA splicing by an IRE1-binding small molecule

Journal: Proceedings of the National Academy of Sciences of the United States of America

doi: 10.1073/pnas.1115623109

Two critical lysines in IRE1 are selectively targeted by 4μ8C. ( A ) Absorption traces of peptides eluting from a C18 reverse-phase HPLC. The column was loaded with a tryptic digest of baculovirus expressed IRE1 that had or had not been exposed
Figure Legend Snippet: Two critical lysines in IRE1 are selectively targeted by 4μ8C. ( A ) Absorption traces of peptides eluting from a C18 reverse-phase HPLC. The column was loaded with a tryptic digest of baculovirus expressed IRE1 that had or had not been exposed

Techniques Used: High Performance Liquid Chromatography

5) Product Images from "Indoleamine 2,3-dioxygenase 1 (IDO1) activity in leukemia blasts correlates with poor outcome in childhood acute myeloid leukemia"

Article Title: Indoleamine 2,3-dioxygenase 1 (IDO1) activity in leukemia blasts correlates with poor outcome in childhood acute myeloid leukemia

Journal: Oncotarget

doi:

Expression and Function of IDO1 in BM Samples from Children with AML BM samples from children with AML obtained at diagnosis were cryopreserved. After thawing, BM mononuclear cells (MNC) were either stimulated with 100 ng/ml IFN-γ for up to 72 hours or were maintained in culture medium alone. Supernatants were collected and used for the measurement of kynurenine and tryptophan levels by RP-HPLC. (A) Up-regulation of IDO protein by IFN-γ (+) in 2 representative AML samples; UPN = Unique Patient Number; Hsp-70 = heat shock protein-70; (B) Release of kynurenine and (C) Consumption of tryptophan by AML blasts maintained in culture for 72 hours with or without exogenous IFN-γ. Blasts from a cohort of 7 children with acute lymphoblastic leukemia (ALL) were also challenged with IFN-γ to detect any IDO-mediated tryptophan breakdown. Comparisons between groups were performed with the Mann-Whitney U test for paired determinations. HC = healthy controls. Medium = blast cells maintained with complete culture medium alone; (D) Time-course experiments with AML blasts from 4 randomly selected BM samples that were either activated with IFN-γ (red dots) or left untouched (black dots). Bars depict the median and interquartile range; (E) Commercially available AML cell lines (see main text for details) were either stimulated with IFN-γ for 72 hours (black columns) or were maintained in culture medium alone (empty columns), prior to HPLC studies. Bars are representative of mean values and standard deviation recorded in 3 independent experiments run in duplicate.
Figure Legend Snippet: Expression and Function of IDO1 in BM Samples from Children with AML BM samples from children with AML obtained at diagnosis were cryopreserved. After thawing, BM mononuclear cells (MNC) were either stimulated with 100 ng/ml IFN-γ for up to 72 hours or were maintained in culture medium alone. Supernatants were collected and used for the measurement of kynurenine and tryptophan levels by RP-HPLC. (A) Up-regulation of IDO protein by IFN-γ (+) in 2 representative AML samples; UPN = Unique Patient Number; Hsp-70 = heat shock protein-70; (B) Release of kynurenine and (C) Consumption of tryptophan by AML blasts maintained in culture for 72 hours with or without exogenous IFN-γ. Blasts from a cohort of 7 children with acute lymphoblastic leukemia (ALL) were also challenged with IFN-γ to detect any IDO-mediated tryptophan breakdown. Comparisons between groups were performed with the Mann-Whitney U test for paired determinations. HC = healthy controls. Medium = blast cells maintained with complete culture medium alone; (D) Time-course experiments with AML blasts from 4 randomly selected BM samples that were either activated with IFN-γ (red dots) or left untouched (black dots). Bars depict the median and interquartile range; (E) Commercially available AML cell lines (see main text for details) were either stimulated with IFN-γ for 72 hours (black columns) or were maintained in culture medium alone (empty columns), prior to HPLC studies. Bars are representative of mean values and standard deviation recorded in 3 independent experiments run in duplicate.

Techniques Used: Expressing, High Performance Liquid Chromatography, MANN-WHITNEY, Standard Deviation

6) Product Images from "Solenodon genome reveals convergent evolution of venom in eulipotyphlan mammals"

Article Title: Solenodon genome reveals convergent evolution of venom in eulipotyphlan mammals

Journal: Proceedings of the National Academy of Sciences of the United States of America

doi: 10.1073/pnas.1906117116

Proteomic analyses of Hispaniolan solenodon ( S. paradoxus ) venom and saliva reveal KLK1 proteins as major venom components. ( A ) Reduced SDS-PAGE gel electrophoretic profiles of venom and saliva samples. ( B ) Gene ontology (GO) term analysis of proteins identified via shotgun proteomic-based annotation to the genome. GO term categories are only displayed for those with at least 2 matches. ( C ) Venn diagram displaying the number of proteins in the venom and saliva, and those identified in both samples via shotgun proteomic-based annotation to the genome. ( D ) Reverse-phase chromatographic separation of venom. Venom was separated by semipreparative reversed-phase HPLC (UV 214nm ) and manually collected. Peptides were directly submitted to LC-MS/MS, whereas protein fractions were analyzed by SDS-PAGE ( Inset ) under reducing conditions. Afterward, protein bands were subjected to in-gel trypsin digestion and identified by spectrum peptide matching against the translated S. paradoxus genome database. ( E and F ) LC-top-down MS analysis of saliva ( E ) and venom ( F ). The peak nomenclature is based on the chromatogram fractions, shown in D . ( E ) Total ion current (TIC) profile of native saliva separated by HPLC. ( F ) TIC profile of native venom separated by HPLC. ( G ) Summary table of the proteins identified via top-down and bottom-up proteomic analyses of solenodon venom, including their mass, corresponding identification in the genome (genome ID), and protein annotation. All identified proteins are annotated as KLK1 , with the exception of keratins, which are human contaminants. ( H ) Comparison of the relative abundance of main proteins present in chromatographic fractions of venom and saliva from top-down MS experiments. SI Appendix , Table S2 presents a summary of the protein matches identified in solenodon venom and saliva via the various proteomic approaches.
Figure Legend Snippet: Proteomic analyses of Hispaniolan solenodon ( S. paradoxus ) venom and saliva reveal KLK1 proteins as major venom components. ( A ) Reduced SDS-PAGE gel electrophoretic profiles of venom and saliva samples. ( B ) Gene ontology (GO) term analysis of proteins identified via shotgun proteomic-based annotation to the genome. GO term categories are only displayed for those with at least 2 matches. ( C ) Venn diagram displaying the number of proteins in the venom and saliva, and those identified in both samples via shotgun proteomic-based annotation to the genome. ( D ) Reverse-phase chromatographic separation of venom. Venom was separated by semipreparative reversed-phase HPLC (UV 214nm ) and manually collected. Peptides were directly submitted to LC-MS/MS, whereas protein fractions were analyzed by SDS-PAGE ( Inset ) under reducing conditions. Afterward, protein bands were subjected to in-gel trypsin digestion and identified by spectrum peptide matching against the translated S. paradoxus genome database. ( E and F ) LC-top-down MS analysis of saliva ( E ) and venom ( F ). The peak nomenclature is based on the chromatogram fractions, shown in D . ( E ) Total ion current (TIC) profile of native saliva separated by HPLC. ( F ) TIC profile of native venom separated by HPLC. ( G ) Summary table of the proteins identified via top-down and bottom-up proteomic analyses of solenodon venom, including their mass, corresponding identification in the genome (genome ID), and protein annotation. All identified proteins are annotated as KLK1 , with the exception of keratins, which are human contaminants. ( H ) Comparison of the relative abundance of main proteins present in chromatographic fractions of venom and saliva from top-down MS experiments. SI Appendix , Table S2 presents a summary of the protein matches identified in solenodon venom and saliva via the various proteomic approaches.

Techniques Used: SDS Page, High Performance Liquid Chromatography, Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry

7) Product Images from "Anthocyanins Extracted from Oryza sativa L. Prevent Fluorouracil-Induced Nuclear Factor-κB Activation in Oral Mucositis: In Vitro and In Vivo Studies"

Article Title: Anthocyanins Extracted from Oryza sativa L. Prevent Fluorouracil-Induced Nuclear Factor-κB Activation in Oral Mucositis: In Vitro and In Vivo Studies

Journal: International Journal of Molecular Sciences

doi: 10.3390/ijms19102981

HPLC-electrospray ionization (ESI) mass spectrometry (MS) analysis of anthrocyanins (ANTs) in Oryza sativa L. ( A ) Representative HPLC chromatograms of Cyanidin-3-glucoside (C3G) and Pelargonidin-3-glucoside (P3G) in the extracts at 530 nm. Peaks were detected with a retention time at 31.0 and 37.0 min, identified as C3G and P3G, respectively; ( B ) Fragmentation patterns in the mass spectra of C3G and P3G in the ANT. The assay was performed in triplicate.
Figure Legend Snippet: HPLC-electrospray ionization (ESI) mass spectrometry (MS) analysis of anthrocyanins (ANTs) in Oryza sativa L. ( A ) Representative HPLC chromatograms of Cyanidin-3-glucoside (C3G) and Pelargonidin-3-glucoside (P3G) in the extracts at 530 nm. Peaks were detected with a retention time at 31.0 and 37.0 min, identified as C3G and P3G, respectively; ( B ) Fragmentation patterns in the mass spectra of C3G and P3G in the ANT. The assay was performed in triplicate.

Techniques Used: High Performance Liquid Chromatography, Mass Spectrometry

8) Product Images from "Anti-tumor activity of nanomicelles encapsulating CXCR4 peptide antagonist E5"

Article Title: Anti-tumor activity of nanomicelles encapsulating CXCR4 peptide antagonist E5

Journal: PLoS ONE

doi: 10.1371/journal.pone.0182697

Characterization of micelles in terms of particle size distribution, morphology and drug release kinetics. (a ) Particle sizes of the PEG-PE micelle (50 μM), M-E5 (PEG-PE: 50 μM, E5: 12.5 μM) and M-E5-Dox (PEG-PE: 50 μM, E5: 12.5 μM, and Dox: 5 μM) were determined by DLS. ( b ) The morphology of the PEG-PE micelle (50 μM), M-E5 (PEG-PE: 50 μM, E5: 12.5 μM) and M-E5-Dox (PEG-PE: 50 μM, E5: 12.5 μM, and Dox: 5 μM) was observed via TEM, and the samples were stained with 1% uranyl acetate for 1 min at room temperature. Scale bar = 100 nm. ( c ) The HPLC chromatogram of Dox, and physicochemical properties of the PEG-PE micelle (100 μM), M-E5 (PEG-PE: 100 μM, E5: 25 μM) and M-E5-Dox (PEG-PE: 100 μM, E5: 25 μM, and Dox: 10 μM). ( d ) Time course (0–72 h) release profiles of Dox and E5 from M-E5-Dox (PEG-PE: 100 μM, E5: 25 μM, and Dox: 10 μM) at 37°C and at pH 5.0 and 7.4. Data are presented as mean ± SD ( n = 3). The * represents significant difference between two groups (*p
Figure Legend Snippet: Characterization of micelles in terms of particle size distribution, morphology and drug release kinetics. (a ) Particle sizes of the PEG-PE micelle (50 μM), M-E5 (PEG-PE: 50 μM, E5: 12.5 μM) and M-E5-Dox (PEG-PE: 50 μM, E5: 12.5 μM, and Dox: 5 μM) were determined by DLS. ( b ) The morphology of the PEG-PE micelle (50 μM), M-E5 (PEG-PE: 50 μM, E5: 12.5 μM) and M-E5-Dox (PEG-PE: 50 μM, E5: 12.5 μM, and Dox: 5 μM) was observed via TEM, and the samples were stained with 1% uranyl acetate for 1 min at room temperature. Scale bar = 100 nm. ( c ) The HPLC chromatogram of Dox, and physicochemical properties of the PEG-PE micelle (100 μM), M-E5 (PEG-PE: 100 μM, E5: 25 μM) and M-E5-Dox (PEG-PE: 100 μM, E5: 25 μM, and Dox: 10 μM). ( d ) Time course (0–72 h) release profiles of Dox and E5 from M-E5-Dox (PEG-PE: 100 μM, E5: 25 μM, and Dox: 10 μM) at 37°C and at pH 5.0 and 7.4. Data are presented as mean ± SD ( n = 3). The * represents significant difference between two groups (*p

Techniques Used: Transmission Electron Microscopy, Staining, High Performance Liquid Chromatography

9) Product Images from "Metabolic Regulation as a Consequence of Anaerobic 5-Methylthioadenosine Recycling in Rhodospirillum rubrum"

Article Title: Metabolic Regulation as a Consequence of Anaerobic 5-Methylthioadenosine Recycling in Rhodospirillum rubrum

Journal: mBio

doi: 10.1128/mBio.00855-16

HPLC identification of purines resulting from MTA metabolism. The R. rubrum wild-type strain was grown anaerobically in the presence of sulfate and then fed with MTA for the indicated amount of time (minutes) before resolution of metabolites via 260-nm absorbance present in the medium after reverse-phase liquid chromatography. “Standard” (black line) is the retention time of known purine base and nucleoside standards (see Fig. S4A in the supplemental material). Ura, urate; Hyx, hypoxanthine; Xan, xanthine; Ino, inosine; Ade, adenine; Xao, xanthosine; Ado, adenosine; MTA, 5-methylthioadenosine.
Figure Legend Snippet: HPLC identification of purines resulting from MTA metabolism. The R. rubrum wild-type strain was grown anaerobically in the presence of sulfate and then fed with MTA for the indicated amount of time (minutes) before resolution of metabolites via 260-nm absorbance present in the medium after reverse-phase liquid chromatography. “Standard” (black line) is the retention time of known purine base and nucleoside standards (see Fig. S4A in the supplemental material). Ura, urate; Hyx, hypoxanthine; Xan, xanthine; Ino, inosine; Ade, adenine; Xao, xanthosine; Ado, adenosine; MTA, 5-methylthioadenosine.

Techniques Used: High Performance Liquid Chromatography, Liquid Chromatography

10) Product Images from "Identification of major matrix metalloproteinase-20 proteolytic processing products of murine amelogenin and tyrosine-rich amelogenin peptide using a nuclear magnetic resonance spectroscopy based method"

Article Title: Identification of major matrix metalloproteinase-20 proteolytic processing products of murine amelogenin and tyrosine-rich amelogenin peptide using a nuclear magnetic resonance spectroscopy based method

Journal: Archives of oral biology

doi: 10.1016/j.archoralbio.2018.06.001

(A) Overlay of the HPLC chromatograms of nTRAP (black dashed line) and following digestion with 3C protease (light blue) to generate rTRAP. (B) The HPLC chromatograms following the incubation of rTRAP with MMP20 for 24 (blue and red) and 120 hours (green). The chromatograms at 24 hour are for the products in the soluble fraction following centrifugation (red) and the pellet (blue) re-suspended in 2% acetic acid. After 120 hours, products were only observed in the soluble fraction following centrifugation. The products in HPLC bands labeled 1 through 4 were collected, lyophilized, and then analyzed by NMR spectroscopy.
Figure Legend Snippet: (A) Overlay of the HPLC chromatograms of nTRAP (black dashed line) and following digestion with 3C protease (light blue) to generate rTRAP. (B) The HPLC chromatograms following the incubation of rTRAP with MMP20 for 24 (blue and red) and 120 hours (green). The chromatograms at 24 hour are for the products in the soluble fraction following centrifugation (red) and the pellet (blue) re-suspended in 2% acetic acid. After 120 hours, products were only observed in the soluble fraction following centrifugation. The products in HPLC bands labeled 1 through 4 were collected, lyophilized, and then analyzed by NMR spectroscopy.

Techniques Used: High Performance Liquid Chromatography, Incubation, Centrifugation, Labeling, Nuclear Magnetic Resonance, Spectroscopy

(A) HPLC chromatograms after a 72 hour incubation of M179 with MMP20. The blue chromatogram is the entire MMP20 digestion mixture solubilized with 2% acetic acid solution and the red chromatogram is the soluble fraction after centrifugation. The products in bands labeled 1 through 5 represent late products generated by the digestion of M179 with MMP20 that were collected, lyophilized, and then analyzed by NMR spectrometry. (B) The HPLC chromatogram of the products in the pellet after centrifugation of the 72 hour MMP20 digestion mixture of M179. The pellet was solubilized in 2% acetic acid. The data was collected with a shallower gradient, and therefore, the time in Figure B is shifted plus 10 minutes per point.
Figure Legend Snippet: (A) HPLC chromatograms after a 72 hour incubation of M179 with MMP20. The blue chromatogram is the entire MMP20 digestion mixture solubilized with 2% acetic acid solution and the red chromatogram is the soluble fraction after centrifugation. The products in bands labeled 1 through 5 represent late products generated by the digestion of M179 with MMP20 that were collected, lyophilized, and then analyzed by NMR spectrometry. (B) The HPLC chromatogram of the products in the pellet after centrifugation of the 72 hour MMP20 digestion mixture of M179. The pellet was solubilized in 2% acetic acid. The data was collected with a shallower gradient, and therefore, the time in Figure B is shifted plus 10 minutes per point.

Techniques Used: High Performance Liquid Chromatography, Incubation, Centrifugation, Labeling, Generated, Nuclear Magnetic Resonance

11) Product Images from "Nitric Oxide Deficiency Accelerates Chlorophyll Breakdown and Stability Loss of Thylakoid Membranes during Dark-Induced Leaf Senescence in Arabidopsis"

Article Title: Nitric Oxide Deficiency Accelerates Chlorophyll Breakdown and Stability Loss of Thylakoid Membranes during Dark-Induced Leaf Senescence in Arabidopsis

Journal: PLoS ONE

doi: 10.1371/journal.pone.0056345

Activities of PAO in wild type and nos1/noa1 leaves during dark-induced leaf senescence. HPLC analysis of pFCC-1 generated by PAO-RCCR coupled assay with crude extracts of PAO and RCCR from wild type and nos1/noa1 leaves during a 4-d dark treatment. pFCC-1 was eluted after 9 min, as indicated by arrows. The experiment was repeated once with qualitatively identical results.
Figure Legend Snippet: Activities of PAO in wild type and nos1/noa1 leaves during dark-induced leaf senescence. HPLC analysis of pFCC-1 generated by PAO-RCCR coupled assay with crude extracts of PAO and RCCR from wild type and nos1/noa1 leaves during a 4-d dark treatment. pFCC-1 was eluted after 9 min, as indicated by arrows. The experiment was repeated once with qualitatively identical results.

Techniques Used: High Performance Liquid Chromatography, Generated

12) Product Images from "Substrate-Induced Inactivation of the Escherichia coli AmiD N-Acetylmuramoyl-l-Alanine Amidase Highlights a New Strategy To Inhibit This Class of Enzyme ▿"

Article Title: Substrate-Induced Inactivation of the Escherichia coli AmiD N-Acetylmuramoyl-l-Alanine Amidase Highlights a New Strategy To Inhibit This Class of Enzyme ▿

Journal: Antimicrobial Agents and Chemotherapy

doi: 10.1128/AAC.01520-07

Release of peptides from the peptidoglycan polymer by the purified AmiD-His 6 . Purified peptidoglycan from E. coli was digested overnight by AmiD-His 6 , and the reaction mixture was analyzed using HPLC and a Nucleosil 100C 18 column as described in Materials
Figure Legend Snippet: Release of peptides from the peptidoglycan polymer by the purified AmiD-His 6 . Purified peptidoglycan from E. coli was digested overnight by AmiD-His 6 , and the reaction mixture was analyzed using HPLC and a Nucleosil 100C 18 column as described in Materials

Techniques Used: Purification, High Performance Liquid Chromatography

13) Product Images from "Activation of 6-Alkoxy-Substituted Methylenecyclopropane Nucleoside Analogs Requires Enzymatic Modification by Adenosine Deaminase-Like Protein 1"

Article Title: Activation of 6-Alkoxy-Substituted Methylenecyclopropane Nucleoside Analogs Requires Enzymatic Modification by Adenosine Deaminase-Like Protein 1

Journal: Antimicrobial Agents and Chemotherapy

doi: 10.1128/AAC.01301-19

Metabolite identification assay. MBX-2168 was exposed to mouse liver microsomes (MLMS), and metabolites were identified by LC-MS/MS analysis. (a) HPLC traces, including UV absorbance at 254 nm and extracted ion chromatographs representing all major metabolites. (b) Structures of notable peaks and relevant MS fragments. HPLC peak 1, synguanol metabolite; HPLC peak 2, metabolic product of oxidation of the butyl chain, identified by the presence of a synguanol MS fragment (peak at m / z 308.3 is from an isotope with higher molecular weight); HPLC peak 3, metabolic product of hydration at the cyclopropylidine substituent, identified by the presence of a MS fragment ( m / z 208.2); HPLC peak 4, metabolic product of oxidation at the core or cyclopropylidine substituent, identified by the presence of an oxidized synguanol MS fragment; HPLC peak 5, parent, MBX-2168 accompanied by significant levels of a synguanol MS fragment.
Figure Legend Snippet: Metabolite identification assay. MBX-2168 was exposed to mouse liver microsomes (MLMS), and metabolites were identified by LC-MS/MS analysis. (a) HPLC traces, including UV absorbance at 254 nm and extracted ion chromatographs representing all major metabolites. (b) Structures of notable peaks and relevant MS fragments. HPLC peak 1, synguanol metabolite; HPLC peak 2, metabolic product of oxidation of the butyl chain, identified by the presence of a synguanol MS fragment (peak at m / z 308.3 is from an isotope with higher molecular weight); HPLC peak 3, metabolic product of hydration at the cyclopropylidine substituent, identified by the presence of a MS fragment ( m / z 208.2); HPLC peak 4, metabolic product of oxidation at the core or cyclopropylidine substituent, identified by the presence of an oxidized synguanol MS fragment; HPLC peak 5, parent, MBX-2168 accompanied by significant levels of a synguanol MS fragment.

Techniques Used: Liquid Chromatography with Mass Spectroscopy, High Performance Liquid Chromatography, Molecular Weight

Enzymatic conversion of MBX-2168-MP to synguanol-MP by ADAL-1. The time-dependent formation of synguanol-MP (a) or IMP (b) was determined by incubating 100 μM MBX-2168-MP (a) or N 6 -methyl-AMP (NAMP) (b), respectively, with purified ADAL-1 and separating and quantifying the products via HPLC. The values represent the mean ± standard deviation from at least three experiments.
Figure Legend Snippet: Enzymatic conversion of MBX-2168-MP to synguanol-MP by ADAL-1. The time-dependent formation of synguanol-MP (a) or IMP (b) was determined by incubating 100 μM MBX-2168-MP (a) or N 6 -methyl-AMP (NAMP) (b), respectively, with purified ADAL-1 and separating and quantifying the products via HPLC. The values represent the mean ± standard deviation from at least three experiments.

Techniques Used: Purification, High Performance Liquid Chromatography, Standard Deviation

14) Product Images from "Utility of Muropeptide Ligase for Identification of Inhibitors of the Cell Wall Biosynthesis Enzyme MurF"

Article Title: Utility of Muropeptide Ligase for Identification of Inhibitors of the Cell Wall Biosynthesis Enzyme MurF

Journal:

doi: 10.1128/AAC.50.1.230-236.2006

HPLC chromatograms of Mpl and MurF reactions. The HPLC profiles at 260 nM are displayed for the following reactions: l -Ala-γ- d -Glu-A 2 pm without enzyme (A) or incubated with Mpl (B) or with Mpl and MurF (F), l -Ala-γ- d -Glu- l -Lys incubated
Figure Legend Snippet: HPLC chromatograms of Mpl and MurF reactions. The HPLC profiles at 260 nM are displayed for the following reactions: l -Ala-γ- d -Glu-A 2 pm without enzyme (A) or incubated with Mpl (B) or with Mpl and MurF (F), l -Ala-γ- d -Glu- l -Lys incubated

Techniques Used: High Performance Liquid Chromatography, Incubation

15) Product Images from "Venomics and antivenomics of the poorly studied Brazil’s lancehead,Bothrops brazili (Hoge, 1954), from the Brazilian State of Pará"

Article Title: Venomics and antivenomics of the poorly studied Brazil’s lancehead,Bothrops brazili (Hoge, 1954), from the Brazilian State of Pará

Journal: The Journal of Venomous Animals and Toxins Including Tropical Diseases

doi: 10.1590/1678-9199-JVATITD-2019-0103

Comparative immunorecognition ability of the Brazilian SAB antivenom towards B. brazili and B. jararaca venom toxins. (A) Third-generation antivenomic analyses of B. brazili and (B) B. jararaca venom with the pentabothropic antivenom ( soro antibotrópico , SAB) produced at Butantan Institute. Reverse-phase chromatographic analysis of whole venom (panels a ) and of the non-retained and the immunoretained fractions recovered from affinity column [9 mg immobilized SAB antivenom F(ab’) 2 molecules] incubated with increasing amounts (300-3600 µg) of venom from ( A ) B. brazili (Pará, Brazil) and ( B ) B. jararaca (SE population) are displayed in panels b through i . Panels j-l show reverse-phase HPLC separations of the retained and non-retained venom fractions on mock matrix and naïve equine IgG affinity columns, respectively.
Figure Legend Snippet: Comparative immunorecognition ability of the Brazilian SAB antivenom towards B. brazili and B. jararaca venom toxins. (A) Third-generation antivenomic analyses of B. brazili and (B) B. jararaca venom with the pentabothropic antivenom ( soro antibotrópico , SAB) produced at Butantan Institute. Reverse-phase chromatographic analysis of whole venom (panels a ) and of the non-retained and the immunoretained fractions recovered from affinity column [9 mg immobilized SAB antivenom F(ab’) 2 molecules] incubated with increasing amounts (300-3600 µg) of venom from ( A ) B. brazili (Pará, Brazil) and ( B ) B. jararaca (SE population) are displayed in panels b through i . Panels j-l show reverse-phase HPLC separations of the retained and non-retained venom fractions on mock matrix and naïve equine IgG affinity columns, respectively.

Techniques Used: Produced, Affinity Column, Incubation, High Performance Liquid Chromatography

16) Product Images from "Exposure of Aspergillus fumigatus to Atorvastatin Leads to Altered Membrane Permeability and Induction of an Oxidative Stress Response"

Article Title: Exposure of Aspergillus fumigatus to Atorvastatin Leads to Altered Membrane Permeability and Induction of an Oxidative Stress Response

Journal: Journal of Fungi

doi: 10.3390/jof6020042

Atorvastatin exposure increased the gliotoxin release from A. fumigatus . Gliotoxin quantification was performed using an HPLC. The gliotoxin standards were used to calibrate the instrument. Gliotoxin content was expressed in terms of ng/mL (* p
Figure Legend Snippet: Atorvastatin exposure increased the gliotoxin release from A. fumigatus . Gliotoxin quantification was performed using an HPLC. The gliotoxin standards were used to calibrate the instrument. Gliotoxin content was expressed in terms of ng/mL (* p

Techniques Used: High Performance Liquid Chromatography

17) Product Images from "Purification and characterization of a novel lipopeptide from Streptomyces amritsarensis sp. nov. active against methicillin-resistant Staphylococcus aureus"

Article Title: Purification and characterization of a novel lipopeptide from Streptomyces amritsarensis sp. nov. active against methicillin-resistant Staphylococcus aureus

Journal: AMB Express

doi: 10.1186/s13568-014-0050-y

Elution profile of lipopeptide using HPLC reverse phase chromatography on ZORBAX 300-SB18 column monitoring by absorbance at 215 nm. Peak 3 corresponds to lipopeptide elution.
Figure Legend Snippet: Elution profile of lipopeptide using HPLC reverse phase chromatography on ZORBAX 300-SB18 column monitoring by absorbance at 215 nm. Peak 3 corresponds to lipopeptide elution.

Techniques Used: High Performance Liquid Chromatography, Reversed-phase Chromatography

18) Product Images from "Impact of Simulated Gastrointestinal Digestion on the Biological Activity of an Alcalase Hydrolysate of Orange Seed (Siavaraze, Citrus sinensis) by-Products"

Article Title: Impact of Simulated Gastrointestinal Digestion on the Biological Activity of an Alcalase Hydrolysate of Orange Seed (Siavaraze, Citrus sinensis) by-Products

Journal: Foods

doi: 10.3390/foods9091217

Reversed-phase high-performance liquid chromatography (RP-HPLC) separation of Fractions (40–44) and (45–49) obtained from SEC. The fractions were automatically collected and assayed for their DPPH scavenging activity and ferric-reducing power ( A ), ACE-inhibitory activity ( B ), and α-amylase-inhibitory activity, and α-glucosidase-inhibitory activity ( C ). Fractions 19 to 20, obtained from RP-HPLC, were selected for further sequencing and identification.
Figure Legend Snippet: Reversed-phase high-performance liquid chromatography (RP-HPLC) separation of Fractions (40–44) and (45–49) obtained from SEC. The fractions were automatically collected and assayed for their DPPH scavenging activity and ferric-reducing power ( A ), ACE-inhibitory activity ( B ), and α-amylase-inhibitory activity, and α-glucosidase-inhibitory activity ( C ). Fractions 19 to 20, obtained from RP-HPLC, were selected for further sequencing and identification.

Techniques Used: High Performance Liquid Chromatography, Activity Assay, Sequencing

Reversed-phase chromatographic separation of F(40–44) and F(45–49) from SEC and after in vitro gastrointestinal digestion. Fractions were automatically collected and assayed for their DPPH scavenging activity and ferric-reducing power ( A ), ACE-inhibitory activity ( B ), and α-amylase-inhibitory activity and α-glucosidase-inhibitory activity ( C ). Fractions 19 and 20 obtained from RP-HPLC were selected for sequencing and identification.
Figure Legend Snippet: Reversed-phase chromatographic separation of F(40–44) and F(45–49) from SEC and after in vitro gastrointestinal digestion. Fractions were automatically collected and assayed for their DPPH scavenging activity and ferric-reducing power ( A ), ACE-inhibitory activity ( B ), and α-amylase-inhibitory activity and α-glucosidase-inhibitory activity ( C ). Fractions 19 and 20 obtained from RP-HPLC were selected for sequencing and identification.

Techniques Used: In Vitro, Activity Assay, High Performance Liquid Chromatography, Sequencing

Related Articles

High Performance Liquid Chromatography:

Article Title: Identification of a Novel O-Conotoxin Reveals an Unusual and Potent Inhibitor of the Human α9α10 Nicotinic Acetylcholine Receptor
Article Snippet: .. The digestion of alkylated GeXXVIIA-L was carried out in 100 mM Tris-HCl, pH 8.5, using 3 μg/mL Asp-N (Sigma, St Louis, MO, USA) at 37 °C for 18 h. The digested products were separated on a ZORBAX C18 HPLC analytical column (4.6 × 250 mm, Agilent). .. Oocyte Two-Electrode-Voltage Clamp Recordings Oocyte preparation, RNA preparation, and expression of nAChR subunits in Xenopus oocytes were performed as described previously [ ].

Article Title: Cancer-targeted design of bioresponsive prodrug with enhanced cellular uptake to achieve precise cancer therapy
Article Snippet: .. HPLC: Agilent 1260 infinity II system, Agilent ZORBAX SB C18 (Santa Clara, CA, USA) (250*4.6 mm, 5 µm) Mobile phase A: H2 O, B: CH3 CN. ..

Article Title: Development of a selective agonist for relaxin family peptide receptor 3
Article Snippet: .. Finally, mature R3/I5 mutants were purified by HPLC using an analytical C18 reverse-phase column (Zorbax 300SB-C18, 4.6 × 250 mm, Agilent Technology) and their identity confirmed by electrospray mass spectrometry on a QTRAP mass spectrometer (Applied Biosystems, Foster City, CA, USA). .. Circular dichroism spectroscopy Mature R3/I5 mutants were dissolved in 1.0 mM aqueous hydrochloride solution (pH 3.0) and their concentrations were determined by absorbance at 280 nm using an extinction coefficient (ε280nm ) of 7365 M−1 ·cm−1 .

Article Title: DigiFab Interacts With Endogenous Cardiotonic Steroids and Reverses Preeclampsia-Induced Na/K-ATPase Inhibition
Article Snippet: .. Plasma samples of 250 μL from each group were pooled, extracted on C-18 cartridges as above, dried, reconstituted in 10% acetonitrile, and fractionated on Agilent 1100 series HPLC system using Agilent Zorbax Eclipse XDB-C18 (Agilent Technologies, Palo Alto, California), 4.6 × 150 mm, 5 μm particle size, 80 Å column, flow rate 1 mL/min, in linear (10%-85.5%) gradient of acetonitrile against 0.1% trifluoroacetic acid for 45 minutes. .. Thirty 1.5-minute fractions were collected and analyzed for MBG immunoreactivity using assays based on 4G4 anti-MBG mAb (above) and on 3E9 anti-MBG mAb, an antibody reported previously to reduce blood pressure in experimental hypertension and to ex vivo reverse PE-induced NKA inhibition, and digoxin-like immunoreactivity using assays based on Digibind and DigiFab.

Article Title: Mechanism for insulin-like peptide 5 distinguishing the homologous relaxin family peptide receptor 3 and 4
Article Snippet: .. Thereafter, the purified folded precursors were sequentially treated with endoproteinase Lys-C and carboxypeptidase B (papaya glutaminyl cyclase was also used for the R3/I5 mutants) according to our previous procedure , and the resultant two-chain INSL5 and R3/I5 mutants were purified by HPLC using an analytical C18 reverse-phase column (Zorbax 300SB-C18, 4.6 × 250 mm, from Agilent Technology). .. The fraction of mature mutant eluted by an acidic acetonitrile gradient was manually collected, lyophilized, and subjected to mass spectrometry analysis.

Flow Cytometry:

Article Title: Synthesis of new potent agonistic analogs of growth hormone-releasing hormone (GHRH) and evaluation of their endocrine and cardiac activities
Article Snippet: .. Peptides were eluted on an Agilent Zorbax C18 column (0.5 mm × 150 mm, 300 Å pore size, 5 μm particle size, Agilent, Santa Clara, CA) at a flow rate of 15 μl/min with a linear gradient from 35 to 85% B for 30 min. Solvent A is 0.1% formic acid (FA), Solvent B is 90% aqueous MeCN/0.1% FA. .. TOF settings are as follow: capillary voltage: 4000 V; drying gas flow: 7 L/min; drying gas temperature: 300 ºC; nebulizer gas: 30 psi; fragmentor voltage: 350 V.

Article Title: DigiFab Interacts With Endogenous Cardiotonic Steroids and Reverses Preeclampsia-Induced Na/K-ATPase Inhibition
Article Snippet: .. Plasma samples of 250 μL from each group were pooled, extracted on C-18 cartridges as above, dried, reconstituted in 10% acetonitrile, and fractionated on Agilent 1100 series HPLC system using Agilent Zorbax Eclipse XDB-C18 (Agilent Technologies, Palo Alto, California), 4.6 × 150 mm, 5 μm particle size, 80 Å column, flow rate 1 mL/min, in linear (10%-85.5%) gradient of acetonitrile against 0.1% trifluoroacetic acid for 45 minutes. .. Thirty 1.5-minute fractions were collected and analyzed for MBG immunoreactivity using assays based on 4G4 anti-MBG mAb (above) and on 3E9 anti-MBG mAb, an antibody reported previously to reduce blood pressure in experimental hypertension and to ex vivo reverse PE-induced NKA inhibition, and digoxin-like immunoreactivity using assays based on Digibind and DigiFab.

Mass Spectrometry:

Article Title: Development of a selective agonist for relaxin family peptide receptor 3
Article Snippet: .. Finally, mature R3/I5 mutants were purified by HPLC using an analytical C18 reverse-phase column (Zorbax 300SB-C18, 4.6 × 250 mm, Agilent Technology) and their identity confirmed by electrospray mass spectrometry on a QTRAP mass spectrometer (Applied Biosystems, Foster City, CA, USA). .. Circular dichroism spectroscopy Mature R3/I5 mutants were dissolved in 1.0 mM aqueous hydrochloride solution (pH 3.0) and their concentrations were determined by absorbance at 280 nm using an extinction coefficient (ε280nm ) of 7365 M−1 ·cm−1 .

Chromatography:

Article Title: Detection of 7-Dehydrocholesterol and Vitamin D3 Derivatives in Honey
Article Snippet: .. Chromatography for LC-MS was performed using a Zorbax Eclipse Plus C18 column (2.1 × 50 mm, 1.8 μm) (Agilent Technology, Santa Clara, CA, USA), an ACQUITY UPLC BEH C18 column (2.1 × 50 mm, 1.7 μm), an Atlantis C18 column (100 × 4.6 mm, 5 μm) (Waters, Milford, MA, USA) or a Pursuit 200Å PFP column (4.6 × 150 mm, 5 µm) (Agilent Technology, Santa Clara, CA, USA). ..

Purification:

Article Title: Development of a selective agonist for relaxin family peptide receptor 3
Article Snippet: .. Finally, mature R3/I5 mutants were purified by HPLC using an analytical C18 reverse-phase column (Zorbax 300SB-C18, 4.6 × 250 mm, Agilent Technology) and their identity confirmed by electrospray mass spectrometry on a QTRAP mass spectrometer (Applied Biosystems, Foster City, CA, USA). .. Circular dichroism spectroscopy Mature R3/I5 mutants were dissolved in 1.0 mM aqueous hydrochloride solution (pH 3.0) and their concentrations were determined by absorbance at 280 nm using an extinction coefficient (ε280nm ) of 7365 M−1 ·cm−1 .

Article Title: Mechanism for insulin-like peptide 5 distinguishing the homologous relaxin family peptide receptor 3 and 4
Article Snippet: .. Thereafter, the purified folded precursors were sequentially treated with endoproteinase Lys-C and carboxypeptidase B (papaya glutaminyl cyclase was also used for the R3/I5 mutants) according to our previous procedure , and the resultant two-chain INSL5 and R3/I5 mutants were purified by HPLC using an analytical C18 reverse-phase column (Zorbax 300SB-C18, 4.6 × 250 mm, from Agilent Technology). .. The fraction of mature mutant eluted by an acidic acetonitrile gradient was manually collected, lyophilized, and subjected to mass spectrometry analysis.

Liquid Chromatography with Mass Spectroscopy:

Article Title: Detection of 7-Dehydrocholesterol and Vitamin D3 Derivatives in Honey
Article Snippet: .. Chromatography for LC-MS was performed using a Zorbax Eclipse Plus C18 column (2.1 × 50 mm, 1.8 μm) (Agilent Technology, Santa Clara, CA, USA), an ACQUITY UPLC BEH C18 column (2.1 × 50 mm, 1.7 μm), an Atlantis C18 column (100 × 4.6 mm, 5 μm) (Waters, Milford, MA, USA) or a Pursuit 200Å PFP column (4.6 × 150 mm, 5 µm) (Agilent Technology, Santa Clara, CA, USA). ..

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    Agilent technologies peptide elution reverse phase high performance liquid chromatography rp hplc purification
    Purification of MHC class II-associated peptides. A. <t>RP-HPLC</t> chromatogram of elution of the MHCII associated peptides. System: Agilent 1100, Column: Agilent ZORBAX 300SB-C18, Flow rate : 1 mL/min and a gradient was created by mixing Solvent A: 0.1% TFA (v/v) in CH3COOH(8.7%) and HCOOH(2.2%), pH1.9, and Solvent B: 0.08% TFA (v/v) in Acetonitrile; B. Dot blot of RP-HPLC fractions. 5 µL from each fraction was applied to a blotting membrane and I-A b molecules were detected as described in the text. C. Quantitative Imaging Analysis of MHCII positive fractions from <t>GILT-WT</t> and GILT−/− samples. MHC class II positive fractions from RP-HPLC were pooled for each sample and three different amounts (high: 25 µL, medium: 12.5 µL, and low: 6µL) from each pool were loaded onto SDS-PAGE gel for quantitative imaging. D. Flow cytometry analysis of GILT−/− and GILT-WT splenocytes. Spleens were isolated, ground and red blood cells lysed in hypertonic buffer. Washed and filtered splenocytes were incubated 30 min. on ice with anti-IA b M5/114–PE antibody.
    Peptide Elution Reverse Phase High Performance Liquid Chromatography Rp Hplc Purification, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Agilent technologies rp hplc purification
    Recombinant expression and characterization of <t>Tgu6.1</t> teretoxin. ( A ) Terebrid snail Terebra guttata from which the Tgu6.1 teretoxin was discovered. ( B ) Plasmid map of Tgu6.1 cloned into pET-32a Xa/ligation independent cloning (LIC) vector via LIC. ( C ) <t>RP-HPLC</t> purification of recombinant Tgu6.1 from its fusion tag after expression, purification and cleavage (top spectra); LC-MS analysis of Tgu6.1 (bottom spectra). ( D ) Characterization of Tgu6.1 bioactivity using the native prey polychaete worm assay (view the video in Supplemental Material ).
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    Agilent technologies agilent rp hplc system
    The purified rhMK was analyzed by SDS-PAGE with protein silver-staining and <t>RP-HPLC</t> (a) 1 μg of purified rhMK column fractions were load on SDS-PAGE and protein silver-staining; no other bands could be observed except the main band of rhMK. Lane M: low M w protein markers; Lanes 1~2: purified rhMK column fractions; (b) Reverse phase HPLC analysis of purified rhMK. Purified rhMK (5 μg) was analyzed by RP-HPLC, using <t>Agilent</t> ZORBAX StableBond-C18 column (150 mm×4.6 mm), which showed a single peak with a retention time of 6.533 min
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    Agilent technologies reverse phase high performance liquid chromatography hplc system
    Binding affinity assays of the selected phages encoding 7-mer peptides for human (HSA) and mouse (MSA) serium albumin, and preparation and identification of recombinant <t>RMP16.</t> ( A ) Selected phages encoding two 7-mer peptides were tested for binding HSA and MSA by ELISA. N12 represents the number of 10 12 phage particles, N11 ∼ N1 is the phage particles number by 4-fold serial dilution from 10 12 . ( B ) The construction map of the expression plasmid pKYB-RMP16. ( C ) The growth curve of the gene engineering E.coli pKYB-RMP16/ER2566. The SDS-PAGE ( D ) and ESI-MS ( E ) analysis of the prepared recombinant RMP16. ( F ) The HLPC analysis of the prepared recombinant RMP16. M: protein marker; 1: The prepared recombinant RMP16. SDS-PAGE: sodium dodecyl sulfate-polyacrylamide gel electrophoresis; <t>HPLC:</t> high-performance liquid chromatography; ESI-MS: electrospray ionization-mass spectrometry.
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    Purification of MHC class II-associated peptides. A. RP-HPLC chromatogram of elution of the MHCII associated peptides. System: Agilent 1100, Column: Agilent ZORBAX 300SB-C18, Flow rate : 1 mL/min and a gradient was created by mixing Solvent A: 0.1% TFA (v/v) in CH3COOH(8.7%) and HCOOH(2.2%), pH1.9, and Solvent B: 0.08% TFA (v/v) in Acetonitrile; B. Dot blot of RP-HPLC fractions. 5 µL from each fraction was applied to a blotting membrane and I-A b molecules were detected as described in the text. C. Quantitative Imaging Analysis of MHCII positive fractions from GILT-WT and GILT−/− samples. MHC class II positive fractions from RP-HPLC were pooled for each sample and three different amounts (high: 25 µL, medium: 12.5 µL, and low: 6µL) from each pool were loaded onto SDS-PAGE gel for quantitative imaging. D. Flow cytometry analysis of GILT−/− and GILT-WT splenocytes. Spleens were isolated, ground and red blood cells lysed in hypertonic buffer. Washed and filtered splenocytes were incubated 30 min. on ice with anti-IA b M5/114–PE antibody.

    Journal: PLoS ONE

    Article Title: Comparative Quantitative Mass Spectrometry Analysis of MHC Class II-Associated Peptides Reveals a Role of GILT in Formation of Self-Peptide Repertoire

    doi: 10.1371/journal.pone.0010599

    Figure Lengend Snippet: Purification of MHC class II-associated peptides. A. RP-HPLC chromatogram of elution of the MHCII associated peptides. System: Agilent 1100, Column: Agilent ZORBAX 300SB-C18, Flow rate : 1 mL/min and a gradient was created by mixing Solvent A: 0.1% TFA (v/v) in CH3COOH(8.7%) and HCOOH(2.2%), pH1.9, and Solvent B: 0.08% TFA (v/v) in Acetonitrile; B. Dot blot of RP-HPLC fractions. 5 µL from each fraction was applied to a blotting membrane and I-A b molecules were detected as described in the text. C. Quantitative Imaging Analysis of MHCII positive fractions from GILT-WT and GILT−/− samples. MHC class II positive fractions from RP-HPLC were pooled for each sample and three different amounts (high: 25 µL, medium: 12.5 µL, and low: 6µL) from each pool were loaded onto SDS-PAGE gel for quantitative imaging. D. Flow cytometry analysis of GILT−/− and GILT-WT splenocytes. Spleens were isolated, ground and red blood cells lysed in hypertonic buffer. Washed and filtered splenocytes were incubated 30 min. on ice with anti-IA b M5/114–PE antibody.

    Article Snippet: Peptide elution Reverse Phase High Performance Liquid Chromatography (RP-HPLC) purification of I-Ab containing GILT-WT and GILT−/− samples was performed on Agilent 1100 Chromatographic system (Agilent Technologies).

    Techniques: Purification, High Performance Liquid Chromatography, Flow Cytometry, Dot Blot, Imaging, SDS Page, Cytometry, Isolation, Incubation, IA

    Recombinant expression and characterization of Tgu6.1 teretoxin. ( A ) Terebrid snail Terebra guttata from which the Tgu6.1 teretoxin was discovered. ( B ) Plasmid map of Tgu6.1 cloned into pET-32a Xa/ligation independent cloning (LIC) vector via LIC. ( C ) RP-HPLC purification of recombinant Tgu6.1 from its fusion tag after expression, purification and cleavage (top spectra); LC-MS analysis of Tgu6.1 (bottom spectra). ( D ) Characterization of Tgu6.1 bioactivity using the native prey polychaete worm assay (view the video in Supplemental Material ).

    Journal: Toxins

    Article Title: Characterization and Recombinant Expression of Terebrid Venom Peptide from Terebra guttata

    doi: 10.3390/toxins8030063

    Figure Lengend Snippet: Recombinant expression and characterization of Tgu6.1 teretoxin. ( A ) Terebrid snail Terebra guttata from which the Tgu6.1 teretoxin was discovered. ( B ) Plasmid map of Tgu6.1 cloned into pET-32a Xa/ligation independent cloning (LIC) vector via LIC. ( C ) RP-HPLC purification of recombinant Tgu6.1 from its fusion tag after expression, purification and cleavage (top spectra); LC-MS analysis of Tgu6.1 (bottom spectra). ( D ) Characterization of Tgu6.1 bioactivity using the native prey polychaete worm assay (view the video in Supplemental Material ).

    Article Snippet: RP-HPLC Purification and Mass Spectrometry Cleaved Tgu6.1 was purified by RP-HPLC (Agilent, Santa Clara, CA, USA) using an X-Bridge C18 semi-preparative column (10 × 150 mm, 5-µm particle size, Waters Corporation, Milford, MA, USA) pre-equilibrated with 95% Buffer A (0.1% TFA).

    Techniques: Recombinant, Expressing, Plasmid Preparation, Clone Assay, Positron Emission Tomography, Ligation, High Performance Liquid Chromatography, Purification, Liquid Chromatography with Mass Spectroscopy

    Expression and purification of Tgu6.1. ( A ) 12% SDS-PAGE Coomassie-stained gel showing expression and purification of Tgu6.1 fusion protein by Ni-NTA affinity chromatography. M = protein molecular weight marker; Lane 1 = cell lysate; Lane 2 = supernatant post-binding to Ni-NTA resin; Lane 3 = Wash Buffer 1 supernatant; Lane 4 = Wash Buffer 2 supernatant; Lane 5 = imidazole eluted fraction. ( B ) Tris-tricine 16.5% SDS-PAGE Coomassie-stained gel showing Tgu6.1 cleavage by enterokinase. M = protein molecular weight marker; Lanes 1–3, enterokinase cleavage in 1:50, 1:20 and 1:10 dilutions. ( C ) Chromatogram of RP-HPLC purification of Tgu6.1 from TRX fusion tag. An X-Bridge C18 semi-preparative column was used with Buffer A (0.1% TFA) and Buffer B (80% ACN/0.1% TFA). The peptide was eluted with a linear gradient of 5%–75% Buffer B over 30 min at a flow rate of 5 mL/min. ( D ) LC-MS characterization of folded Tgu6.1. The +4, +5, +6 and +7 ion charge states are shown. Expected mass = 4758.58 Da. Observed mass = 4758.28 Da.

    Journal: Toxins

    Article Title: Characterization and Recombinant Expression of Terebrid Venom Peptide from Terebra guttata

    doi: 10.3390/toxins8030063

    Figure Lengend Snippet: Expression and purification of Tgu6.1. ( A ) 12% SDS-PAGE Coomassie-stained gel showing expression and purification of Tgu6.1 fusion protein by Ni-NTA affinity chromatography. M = protein molecular weight marker; Lane 1 = cell lysate; Lane 2 = supernatant post-binding to Ni-NTA resin; Lane 3 = Wash Buffer 1 supernatant; Lane 4 = Wash Buffer 2 supernatant; Lane 5 = imidazole eluted fraction. ( B ) Tris-tricine 16.5% SDS-PAGE Coomassie-stained gel showing Tgu6.1 cleavage by enterokinase. M = protein molecular weight marker; Lanes 1–3, enterokinase cleavage in 1:50, 1:20 and 1:10 dilutions. ( C ) Chromatogram of RP-HPLC purification of Tgu6.1 from TRX fusion tag. An X-Bridge C18 semi-preparative column was used with Buffer A (0.1% TFA) and Buffer B (80% ACN/0.1% TFA). The peptide was eluted with a linear gradient of 5%–75% Buffer B over 30 min at a flow rate of 5 mL/min. ( D ) LC-MS characterization of folded Tgu6.1. The +4, +5, +6 and +7 ion charge states are shown. Expected mass = 4758.58 Da. Observed mass = 4758.28 Da.

    Article Snippet: RP-HPLC Purification and Mass Spectrometry Cleaved Tgu6.1 was purified by RP-HPLC (Agilent, Santa Clara, CA, USA) using an X-Bridge C18 semi-preparative column (10 × 150 mm, 5-µm particle size, Waters Corporation, Milford, MA, USA) pre-equilibrated with 95% Buffer A (0.1% TFA).

    Techniques: Expressing, Purification, SDS Page, Staining, Affinity Chromatography, Molecular Weight, Marker, Binding Assay, High Performance Liquid Chromatography, Flow Cytometry, Liquid Chromatography with Mass Spectroscopy

    The purified rhMK was analyzed by SDS-PAGE with protein silver-staining and RP-HPLC (a) 1 μg of purified rhMK column fractions were load on SDS-PAGE and protein silver-staining; no other bands could be observed except the main band of rhMK. Lane M: low M w protein markers; Lanes 1~2: purified rhMK column fractions; (b) Reverse phase HPLC analysis of purified rhMK. Purified rhMK (5 μg) was analyzed by RP-HPLC, using Agilent ZORBAX StableBond-C18 column (150 mm×4.6 mm), which showed a single peak with a retention time of 6.533 min

    Journal: Journal of Zhejiang University. Science. B

    Article Title: Expression and purification of bioactive high-purity human midkine in Escherichia coli *

    doi: 10.1631/jzus.B0820385

    Figure Lengend Snippet: The purified rhMK was analyzed by SDS-PAGE with protein silver-staining and RP-HPLC (a) 1 μg of purified rhMK column fractions were load on SDS-PAGE and protein silver-staining; no other bands could be observed except the main band of rhMK. Lane M: low M w protein markers; Lanes 1~2: purified rhMK column fractions; (b) Reverse phase HPLC analysis of purified rhMK. Purified rhMK (5 μg) was analyzed by RP-HPLC, using Agilent ZORBAX StableBond-C18 column (150 mm×4.6 mm), which showed a single peak with a retention time of 6.533 min

    Article Snippet: The purity of the fractions was analyzed by an Agilent RP-HPLC system.

    Techniques: Purification, SDS Page, Silver Staining, High Performance Liquid Chromatography

    Binding affinity assays of the selected phages encoding 7-mer peptides for human (HSA) and mouse (MSA) serium albumin, and preparation and identification of recombinant RMP16. ( A ) Selected phages encoding two 7-mer peptides were tested for binding HSA and MSA by ELISA. N12 represents the number of 10 12 phage particles, N11 ∼ N1 is the phage particles number by 4-fold serial dilution from 10 12 . ( B ) The construction map of the expression plasmid pKYB-RMP16. ( C ) The growth curve of the gene engineering E.coli pKYB-RMP16/ER2566. The SDS-PAGE ( D ) and ESI-MS ( E ) analysis of the prepared recombinant RMP16. ( F ) The HLPC analysis of the prepared recombinant RMP16. M: protein marker; 1: The prepared recombinant RMP16. SDS-PAGE: sodium dodecyl sulfate-polyacrylamide gel electrophoresis; HPLC: high-performance liquid chromatography; ESI-MS: electrospray ionization-mass spectrometry.

    Journal: Scientific Reports

    Article Title: A novel recombinant slow-release TNF α-derived peptide effectively inhibits tumor growth and angiogensis

    doi: 10.1038/srep13595

    Figure Lengend Snippet: Binding affinity assays of the selected phages encoding 7-mer peptides for human (HSA) and mouse (MSA) serium albumin, and preparation and identification of recombinant RMP16. ( A ) Selected phages encoding two 7-mer peptides were tested for binding HSA and MSA by ELISA. N12 represents the number of 10 12 phage particles, N11 ∼ N1 is the phage particles number by 4-fold serial dilution from 10 12 . ( B ) The construction map of the expression plasmid pKYB-RMP16. ( C ) The growth curve of the gene engineering E.coli pKYB-RMP16/ER2566. The SDS-PAGE ( D ) and ESI-MS ( E ) analysis of the prepared recombinant RMP16. ( F ) The HLPC analysis of the prepared recombinant RMP16. M: protein marker; 1: The prepared recombinant RMP16. SDS-PAGE: sodium dodecyl sulfate-polyacrylamide gel electrophoresis; HPLC: high-performance liquid chromatography; ESI-MS: electrospray ionization-mass spectrometry.

    Article Snippet: After chitin beads affinity chromatography purification for the cell lysate, RMP16 was purified and prepared by reverse-phase high-performance liquid chromatography (HPLC) system using 4.6 mm × 150 mm 300 SB-C18 Sep-Pak column (Agilent Technologies, Beijing, China) through gradient elution with increasing concentration of acetonitrile from 2% to 55% for 50 minutes at 1 ml/min.

    Techniques: Binding Assay, Recombinant, Enzyme-linked Immunosorbent Assay, Serial Dilution, Expressing, Plasmid Preparation, SDS Page, Mass Spectrometry, Marker, Polyacrylamide Gel Electrophoresis, High Performance Liquid Chromatography