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Millipore maldi ms
Characterization of ADP-ribosyl-HNP-1 from BAL fluid by <t>RP-HPLC,</t> <t>MALDI,</t> and enzymatic digestion. ( a ) Alignment of RP-HPLC chromatograms of products of ART-1-catalyzed ADP-ribosylation of HNP-1 (continuous line) and a chromatogram of a BAL sample from a smoker (dotted line). Arrows indicate elution times of ADP-ribosyl-HNP-1 and HNP-1. ( b ) ( i ) The peak with elution time compatible with ADP-ribosyl-HNP-1 (46.5 min), analyzed by MALDI-MS, shows a mass of 3,983 Da, consistent with ADP-ribosyl-HNP-1 (calculated 3,983 Da). ( ii ) Incubation of ADP-ribosyl-HNP-1 with pyrophosphatase and alkaline phosphatase produced ribosyl-HNP-1 (calculated 3,574 Da). ( iii ) ADP-ribosylarginine hydrolase cleaved the ribose-arginine linkage to release HNP-1 (calculated 3,443 Da). m / z is on the x axis.
Maldi Ms, supplied by Millipore, used in various techniques. Bioz Stars score: 91/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "ADP ribosylation of human neutrophil peptide-1 regulates its biological properties"

Article Title: ADP ribosylation of human neutrophil peptide-1 regulates its biological properties

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

doi: 10.1073/pnas.122238899

Characterization of ADP-ribosyl-HNP-1 from BAL fluid by RP-HPLC, MALDI, and enzymatic digestion. ( a ) Alignment of RP-HPLC chromatograms of products of ART-1-catalyzed ADP-ribosylation of HNP-1 (continuous line) and a chromatogram of a BAL sample from a smoker (dotted line). Arrows indicate elution times of ADP-ribosyl-HNP-1 and HNP-1. ( b ) ( i ) The peak with elution time compatible with ADP-ribosyl-HNP-1 (46.5 min), analyzed by MALDI-MS, shows a mass of 3,983 Da, consistent with ADP-ribosyl-HNP-1 (calculated 3,983 Da). ( ii ) Incubation of ADP-ribosyl-HNP-1 with pyrophosphatase and alkaline phosphatase produced ribosyl-HNP-1 (calculated 3,574 Da). ( iii ) ADP-ribosylarginine hydrolase cleaved the ribose-arginine linkage to release HNP-1 (calculated 3,443 Da). m / z is on the x axis.
Figure Legend Snippet: Characterization of ADP-ribosyl-HNP-1 from BAL fluid by RP-HPLC, MALDI, and enzymatic digestion. ( a ) Alignment of RP-HPLC chromatograms of products of ART-1-catalyzed ADP-ribosylation of HNP-1 (continuous line) and a chromatogram of a BAL sample from a smoker (dotted line). Arrows indicate elution times of ADP-ribosyl-HNP-1 and HNP-1. ( b ) ( i ) The peak with elution time compatible with ADP-ribosyl-HNP-1 (46.5 min), analyzed by MALDI-MS, shows a mass of 3,983 Da, consistent with ADP-ribosyl-HNP-1 (calculated 3,983 Da). ( ii ) Incubation of ADP-ribosyl-HNP-1 with pyrophosphatase and alkaline phosphatase produced ribosyl-HNP-1 (calculated 3,574 Da). ( iii ) ADP-ribosylarginine hydrolase cleaved the ribose-arginine linkage to release HNP-1 (calculated 3,443 Da). m / z is on the x axis.

Techniques Used: High Performance Liquid Chromatography, Mass Spectrometry, Incubation, Produced

2) Product Images from "A Novel Therapeutic Approach in the Treatment of Pulmonary Arterial Hypertension: Allium ursinum Liophylisate Alleviates Symptoms Comparably to Sildenafil"

Article Title: A Novel Therapeutic Approach in the Treatment of Pulmonary Arterial Hypertension: Allium ursinum Liophylisate Alleviates Symptoms Comparably to Sildenafil

Journal: International Journal of Molecular Sciences

doi: 10.3390/ijms18071436

Mass Spectrometry results. MALDI-TOF mass spectra of compounds from Allium ursinum leaf liophylisate (WGLL) extracts, using 2,5-Dihydroxybenzoic acid (DHB) matrix. ( A , B ) Compounds previously separated by C18 column; ( A ) Compounds with relatively low molecular weight; B: compounds with higher molecular weight; ( C , D ) components of WGLL extract, previously separated by silica S100 column; ( C ) Compounds with relatively low molecular weight; ( D ) Compounds with higher molecular weight.
Figure Legend Snippet: Mass Spectrometry results. MALDI-TOF mass spectra of compounds from Allium ursinum leaf liophylisate (WGLL) extracts, using 2,5-Dihydroxybenzoic acid (DHB) matrix. ( A , B ) Compounds previously separated by C18 column; ( A ) Compounds with relatively low molecular weight; B: compounds with higher molecular weight; ( C , D ) components of WGLL extract, previously separated by silica S100 column; ( C ) Compounds with relatively low molecular weight; ( D ) Compounds with higher molecular weight.

Techniques Used: Mass Spectrometry, Molecular Weight

3) Product Images from "Multi-modal mass spectrometric imaging of small molecules reveals distinct spatio-molecular signatures in differentially metastatic breast tumor models"

Article Title: Multi-modal mass spectrometric imaging of small molecules reveals distinct spatio-molecular signatures in differentially metastatic breast tumor models

Journal: Cancer research

doi: 10.1158/0008-5472.CAN-10-0360

(A) MALDI-MS microscope mode data set of a representative MDA-MB-231 tumor showing the H E image, the corresponding MS imaging of Cho and PC, and the PCA image of the function +2. (B) SIMS microprobe data set of a representative MCF-7 tumor showing the H E image, the corresponding MS imaging of Cho and PC, and the PCA images of the functions +2 and −2 providing inverse images, in which tumor regions are defined by masses other than Cho and PC. Scale bar: 1 mm
Figure Legend Snippet: (A) MALDI-MS microscope mode data set of a representative MDA-MB-231 tumor showing the H E image, the corresponding MS imaging of Cho and PC, and the PCA image of the function +2. (B) SIMS microprobe data set of a representative MCF-7 tumor showing the H E image, the corresponding MS imaging of Cho and PC, and the PCA images of the functions +2 and −2 providing inverse images, in which tumor regions are defined by masses other than Cho and PC. Scale bar: 1 mm

Techniques Used: Mass Spectrometry, Microscopy, Multiple Displacement Amplification, Imaging

4) Product Images from "A novel function for globulin in sequestering plant hormone: Crystal structure of Wrightia tinctoria 11S globulin in complex with auxin"

Article Title: A novel function for globulin in sequestering plant hormone: Crystal structure of Wrightia tinctoria 11S globulin in complex with auxin

Journal: Scientific Reports

doi: 10.1038/s41598-017-04518-7

Ligand identification of by MALDI-MS and HRMS. ( A ) MALDI-MS spectra profile of pure Indole-3-acetic acid (IAA) acquired from Sigma-Aldrich (magenta) and IAA obtained from denatured WTG sample (blue). The auxin (IAA) corresponds to a molecule with m/z = 175.15 (shown by red arrow). In addition, the spectrum also showed peaks in the low molecular weight range from 100–500 Da indicating peaks corresponding to the matrix ions. ( B ) HRMS profile of sample isolated from purified WTG wild-type protein. ( C ) HRMS profile of standard auxin. A peak at 198.10 corresponding to an m/z ratio of the IAA sodium adduct C 10 H 9 NO 2 Na [M + Na] + was obtained. The red arrow in B and C indicate the m/z ratio of the IAA sodium adduct.
Figure Legend Snippet: Ligand identification of by MALDI-MS and HRMS. ( A ) MALDI-MS spectra profile of pure Indole-3-acetic acid (IAA) acquired from Sigma-Aldrich (magenta) and IAA obtained from denatured WTG sample (blue). The auxin (IAA) corresponds to a molecule with m/z = 175.15 (shown by red arrow). In addition, the spectrum also showed peaks in the low molecular weight range from 100–500 Da indicating peaks corresponding to the matrix ions. ( B ) HRMS profile of sample isolated from purified WTG wild-type protein. ( C ) HRMS profile of standard auxin. A peak at 198.10 corresponding to an m/z ratio of the IAA sodium adduct C 10 H 9 NO 2 Na [M + Na] + was obtained. The red arrow in B and C indicate the m/z ratio of the IAA sodium adduct.

Techniques Used: Mass Spectrometry, Molecular Weight, Isolation, Purification

5) Product Images from "ADP ribosylation of human neutrophil peptide-1 regulates its biological properties"

Article Title: ADP ribosylation of human neutrophil peptide-1 regulates its biological properties

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

doi: 10.1073/pnas.122238899

Characterization of ADP-ribosyl-HNP-1 from BAL fluid by RP-HPLC, MALDI, and enzymatic digestion. ( a ) Alignment of RP-HPLC chromatograms of products of ART-1-catalyzed ADP-ribosylation of HNP-1 (continuous line) and a chromatogram of a BAL sample from a smoker (dotted line). Arrows indicate elution times of ADP-ribosyl-HNP-1 and HNP-1. ( b ) ( i ) The peak with elution time compatible with ADP-ribosyl-HNP-1 (46.5 min), analyzed by MALDI-MS, shows a mass of 3,983 Da, consistent with ADP-ribosyl-HNP-1 (calculated 3,983 Da). ( ii ) Incubation of ADP-ribosyl-HNP-1 with pyrophosphatase and alkaline phosphatase produced ribosyl-HNP-1 (calculated 3,574 Da). ( iii ) ADP-ribosylarginine hydrolase cleaved the ribose-arginine linkage to release HNP-1 (calculated 3,443 Da). m / z is on the x axis.
Figure Legend Snippet: Characterization of ADP-ribosyl-HNP-1 from BAL fluid by RP-HPLC, MALDI, and enzymatic digestion. ( a ) Alignment of RP-HPLC chromatograms of products of ART-1-catalyzed ADP-ribosylation of HNP-1 (continuous line) and a chromatogram of a BAL sample from a smoker (dotted line). Arrows indicate elution times of ADP-ribosyl-HNP-1 and HNP-1. ( b ) ( i ) The peak with elution time compatible with ADP-ribosyl-HNP-1 (46.5 min), analyzed by MALDI-MS, shows a mass of 3,983 Da, consistent with ADP-ribosyl-HNP-1 (calculated 3,983 Da). ( ii ) Incubation of ADP-ribosyl-HNP-1 with pyrophosphatase and alkaline phosphatase produced ribosyl-HNP-1 (calculated 3,574 Da). ( iii ) ADP-ribosylarginine hydrolase cleaved the ribose-arginine linkage to release HNP-1 (calculated 3,443 Da). m / z is on the x axis.

Techniques Used: High Performance Liquid Chromatography, Mass Spectrometry, Incubation, Produced

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    Millipore maldi tof mass spectrometry
    Provision of exogenous reduced HMGB1 increases autophagy in cancer cells (A) Relative amounts of oxidized Cys106 (as Cys sulfonic acid) in Lilly Pool #2 and #3. <t>MALDI-TOF</t> Mass Spectrum of tryptic fragments of Lilly Pool #2 (top) and Pool #3 (bottom). The Cys106 containing fragment is amino acids 97–112. The free sulfhydryl (-SH) of total reducible cysteine is at a mass of 1944.9 Da. The monoxide is faintly seen at a mass of 1960.9 Da. The di- and tri- oxides are at masses of 1976.9 Da and 1992.9 Da, respectively. The peak at 1962.9 Da is the free sulfhydryl of the 13–28 fragments, used as an internal standard to verify the DTT reduction went to completion. (B) Reduced HMGB1 protein induces autophagy and oxidized HMGB1 mildly induces apoptosis. Panc2.03 and HCT116 cancer cells were treated with oxidized HMGB1 (“O”, 10 μg/ml) or reduced HMGB1 (“R”, 10 μg/ml) for 24 h, and then assayed for apoptosis by FACS using Annexin V/PI stain and autophagy by quantification of the percentage of cells with GFP-LC3 dots as described in methods. (C) Western analysis of LC3 processing in the presence or absence of lysosomal protease inhibitors pepstatin A (10 μg/ml) and E64D (10 μg/ml) and degradation of p62 by autophagy after HMGB1 or HMGB1 C106S mutant treatment. (D) Reduced HMGB1 protein regulates Beclin1/Bcl-2 complex formation in autophagy. Panc2.03 cells were treated with oxidized HMGB1 (“O”, 10 μg/ml) or reduced HMGB1 (“R”, 10 μg/ml), for 6 h, then cell lysates were prepared for IP with anti-Beclin1/-Bcl-2 or IgG. The resulting immune complexes and inputs were analyzed by western blotting as indicated. Representative western blotting analysis of protein levels is presented. (E) RAGE/Beclin1 but not TLR4 is required for HMGB1 mediated autophagy. Cells were transfected with the indicated shRNA for 48 h and then were treated with reduced HMGB1 (“R”, 10 μg/ml) for 24 h. Representative western blotting analysis of protein levels is presented. In parallel, autophagy was assayed by the percentage of cells with GFP-LC3 dots (N=3, * p
    Maldi Tof Mass Spectrometry, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 44 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/maldi tof mass spectrometry/product/Millipore
    Average 99 stars, based on 44 article reviews
    Price from $9.99 to $1999.99
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    92
    Millipore maldi ms
    Characterization of ADP-ribosyl-HNP-1 from BAL fluid by <t>RP-HPLC,</t> <t>MALDI,</t> and enzymatic digestion. ( a ) Alignment of RP-HPLC chromatograms of products of ART-1-catalyzed ADP-ribosylation of HNP-1 (continuous line) and a chromatogram of a BAL sample from a smoker (dotted line). Arrows indicate elution times of ADP-ribosyl-HNP-1 and HNP-1. ( b ) ( i ) The peak with elution time compatible with ADP-ribosyl-HNP-1 (46.5 min), analyzed by MALDI-MS, shows a mass of 3,983 Da, consistent with ADP-ribosyl-HNP-1 (calculated 3,983 Da). ( ii ) Incubation of ADP-ribosyl-HNP-1 with pyrophosphatase and alkaline phosphatase produced ribosyl-HNP-1 (calculated 3,574 Da). ( iii ) ADP-ribosylarginine hydrolase cleaved the ribose-arginine linkage to release HNP-1 (calculated 3,443 Da). m / z is on the x axis.
    Maldi Ms, supplied by Millipore, used in various techniques. Bioz Stars score: 92/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/maldi ms/product/Millipore
    Average 92 stars, based on 12 article reviews
    Price from $9.99 to $1999.99
    maldi ms - by Bioz Stars, 2020-08
    92/100 stars
      Buy from Supplier

    90
    Millipore matrix assisted laser desorption ionization time of flight maldi tof
    CAPS is phosphorylated at N- and C-terminal Ser residues. A , <t>MALDI-TOF</t> spectra of CAPS phosphopeptides. Phosphopeptides enriched from CAPS tryptic peptides by Ga(III)- immobilized metal ion affinity chromatography were incubated without ( upper panel )
    Matrix Assisted Laser Desorption Ionization Time Of Flight Maldi Tof, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/matrix assisted laser desorption ionization time of flight maldi tof/product/Millipore
    Average 90 stars, based on 4 article reviews
    Price from $9.99 to $1999.99
    matrix assisted laser desorption ionization time of flight maldi tof - by Bioz Stars, 2020-08
    90/100 stars
      Buy from Supplier

    Image Search Results


    Provision of exogenous reduced HMGB1 increases autophagy in cancer cells (A) Relative amounts of oxidized Cys106 (as Cys sulfonic acid) in Lilly Pool #2 and #3. MALDI-TOF Mass Spectrum of tryptic fragments of Lilly Pool #2 (top) and Pool #3 (bottom). The Cys106 containing fragment is amino acids 97–112. The free sulfhydryl (-SH) of total reducible cysteine is at a mass of 1944.9 Da. The monoxide is faintly seen at a mass of 1960.9 Da. The di- and tri- oxides are at masses of 1976.9 Da and 1992.9 Da, respectively. The peak at 1962.9 Da is the free sulfhydryl of the 13–28 fragments, used as an internal standard to verify the DTT reduction went to completion. (B) Reduced HMGB1 protein induces autophagy and oxidized HMGB1 mildly induces apoptosis. Panc2.03 and HCT116 cancer cells were treated with oxidized HMGB1 (“O”, 10 μg/ml) or reduced HMGB1 (“R”, 10 μg/ml) for 24 h, and then assayed for apoptosis by FACS using Annexin V/PI stain and autophagy by quantification of the percentage of cells with GFP-LC3 dots as described in methods. (C) Western analysis of LC3 processing in the presence or absence of lysosomal protease inhibitors pepstatin A (10 μg/ml) and E64D (10 μg/ml) and degradation of p62 by autophagy after HMGB1 or HMGB1 C106S mutant treatment. (D) Reduced HMGB1 protein regulates Beclin1/Bcl-2 complex formation in autophagy. Panc2.03 cells were treated with oxidized HMGB1 (“O”, 10 μg/ml) or reduced HMGB1 (“R”, 10 μg/ml), for 6 h, then cell lysates were prepared for IP with anti-Beclin1/-Bcl-2 or IgG. The resulting immune complexes and inputs were analyzed by western blotting as indicated. Representative western blotting analysis of protein levels is presented. (E) RAGE/Beclin1 but not TLR4 is required for HMGB1 mediated autophagy. Cells were transfected with the indicated shRNA for 48 h and then were treated with reduced HMGB1 (“R”, 10 μg/ml) for 24 h. Representative western blotting analysis of protein levels is presented. In parallel, autophagy was assayed by the percentage of cells with GFP-LC3 dots (N=3, * p

    Journal: Oncogene

    Article Title: HMGB1 Release and Redox Regulates Autophagy and Apoptosis in Cancer Cells

    doi: 10.1038/onc.2010.261

    Figure Lengend Snippet: Provision of exogenous reduced HMGB1 increases autophagy in cancer cells (A) Relative amounts of oxidized Cys106 (as Cys sulfonic acid) in Lilly Pool #2 and #3. MALDI-TOF Mass Spectrum of tryptic fragments of Lilly Pool #2 (top) and Pool #3 (bottom). The Cys106 containing fragment is amino acids 97–112. The free sulfhydryl (-SH) of total reducible cysteine is at a mass of 1944.9 Da. The monoxide is faintly seen at a mass of 1960.9 Da. The di- and tri- oxides are at masses of 1976.9 Da and 1992.9 Da, respectively. The peak at 1962.9 Da is the free sulfhydryl of the 13–28 fragments, used as an internal standard to verify the DTT reduction went to completion. (B) Reduced HMGB1 protein induces autophagy and oxidized HMGB1 mildly induces apoptosis. Panc2.03 and HCT116 cancer cells were treated with oxidized HMGB1 (“O”, 10 μg/ml) or reduced HMGB1 (“R”, 10 μg/ml) for 24 h, and then assayed for apoptosis by FACS using Annexin V/PI stain and autophagy by quantification of the percentage of cells with GFP-LC3 dots as described in methods. (C) Western analysis of LC3 processing in the presence or absence of lysosomal protease inhibitors pepstatin A (10 μg/ml) and E64D (10 μg/ml) and degradation of p62 by autophagy after HMGB1 or HMGB1 C106S mutant treatment. (D) Reduced HMGB1 protein regulates Beclin1/Bcl-2 complex formation in autophagy. Panc2.03 cells were treated with oxidized HMGB1 (“O”, 10 μg/ml) or reduced HMGB1 (“R”, 10 μg/ml), for 6 h, then cell lysates were prepared for IP with anti-Beclin1/-Bcl-2 or IgG. The resulting immune complexes and inputs were analyzed by western blotting as indicated. Representative western blotting analysis of protein levels is presented. (E) RAGE/Beclin1 but not TLR4 is required for HMGB1 mediated autophagy. Cells were transfected with the indicated shRNA for 48 h and then were treated with reduced HMGB1 (“R”, 10 μg/ml) for 24 h. Representative western blotting analysis of protein levels is presented. In parallel, autophagy was assayed by the percentage of cells with GFP-LC3 dots (N=3, * p

    Article Snippet: MALDI-TOF mass spectrometry For MALDI-TOF Mass Spectrometry sample preparation, solid-phase extraction pipette tips (C18 ZipTip) from Millipore were used.

    Techniques: FACS, Staining, Western Blot, Mutagenesis, Transfection, shRNA

    Characterization of ADP-ribosyl-HNP-1 from BAL fluid by RP-HPLC, MALDI, and enzymatic digestion. ( a ) Alignment of RP-HPLC chromatograms of products of ART-1-catalyzed ADP-ribosylation of HNP-1 (continuous line) and a chromatogram of a BAL sample from a smoker (dotted line). Arrows indicate elution times of ADP-ribosyl-HNP-1 and HNP-1. ( b ) ( i ) The peak with elution time compatible with ADP-ribosyl-HNP-1 (46.5 min), analyzed by MALDI-MS, shows a mass of 3,983 Da, consistent with ADP-ribosyl-HNP-1 (calculated 3,983 Da). ( ii ) Incubation of ADP-ribosyl-HNP-1 with pyrophosphatase and alkaline phosphatase produced ribosyl-HNP-1 (calculated 3,574 Da). ( iii ) ADP-ribosylarginine hydrolase cleaved the ribose-arginine linkage to release HNP-1 (calculated 3,443 Da). m / z is on the x axis.

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

    Article Title: ADP ribosylation of human neutrophil peptide-1 regulates its biological properties

    doi: 10.1073/pnas.122238899

    Figure Lengend Snippet: Characterization of ADP-ribosyl-HNP-1 from BAL fluid by RP-HPLC, MALDI, and enzymatic digestion. ( a ) Alignment of RP-HPLC chromatograms of products of ART-1-catalyzed ADP-ribosylation of HNP-1 (continuous line) and a chromatogram of a BAL sample from a smoker (dotted line). Arrows indicate elution times of ADP-ribosyl-HNP-1 and HNP-1. ( b ) ( i ) The peak with elution time compatible with ADP-ribosyl-HNP-1 (46.5 min), analyzed by MALDI-MS, shows a mass of 3,983 Da, consistent with ADP-ribosyl-HNP-1 (calculated 3,983 Da). ( ii ) Incubation of ADP-ribosyl-HNP-1 with pyrophosphatase and alkaline phosphatase produced ribosyl-HNP-1 (calculated 3,574 Da). ( iii ) ADP-ribosylarginine hydrolase cleaved the ribose-arginine linkage to release HNP-1 (calculated 3,443 Da). m / z is on the x axis.

    Article Snippet: We incubated ADP-ribosyl-HNP-1 (6 pmol/0.2 μg) in 200 μl of 250 mM NaHCO3 /25 mM MgCl2 , alkaline phosphatase (5 μg), and pyrophosphatase (5 μg) (Sigma) for 30 min at 37°C before termination of the reaction with 6 M guanidine, separation of reaction products by RP-HPLC, and analysis by MALDI-MS. We also incubated ADP-ribosyl-HNP-1 (11 pmol, 0.42 μg) overnight at 37°C with recombinant human ADP-ribosylarginine hydrolase (1 μg) in 100 μl of 50 mM Tris (pH 7.5)/5 mM DTT/10 mM Mg Cl2 , followed by desalting and concentration using Zip-TipC18 (Millipore), and analysis by MALDI-MS.

    Techniques: High Performance Liquid Chromatography, Mass Spectrometry, Incubation, Produced

    CAPS is phosphorylated at N- and C-terminal Ser residues. A , MALDI-TOF spectra of CAPS phosphopeptides. Phosphopeptides enriched from CAPS tryptic peptides by Ga(III)- immobilized metal ion affinity chromatography were incubated without ( upper panel )

    Journal: The Journal of Biological Chemistry

    Article Title: CAPS Activity in Priming Vesicle Exocytosis Requires CK2 Phosphorylation *

    doi: 10.1074/jbc.M109.017483

    Figure Lengend Snippet: CAPS is phosphorylated at N- and C-terminal Ser residues. A , MALDI-TOF spectra of CAPS phosphopeptides. Phosphopeptides enriched from CAPS tryptic peptides by Ga(III)- immobilized metal ion affinity chromatography were incubated without ( upper panel )

    Article Snippet: For matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF), samples were prepared with a ZipTip C18 (Millipore) and mixed with matrix (2 mg/ml 2′,4′,6′-trihydroxyacetophenone, 10 m m ammonium citrate, 25% acetonitrile, 0.2% trifluoroacetic acid).

    Techniques: Affinity Chromatography, Incubation