Complex Carbohydrates of Red Wine: Characterization of the Extreme Diversity of Neutral Oligosaccharides by ESI-MS

2015 ◽  
Vol 63 (2) ◽  
pp. 671-682 ◽  
Author(s):  
Thierry Doco ◽  
Pascale Williams ◽  
Emmanuelle Meudec ◽  
Véronique Cheynier ◽  
Nicolas Sommerer
Keyword(s):  
Red Wine ◽  
Esi Ms ◽  
Complex Carbohydrates

Characterization of thirty-nine polymethoxylated flavonoids (PMFs) in the branches of Murraya paniculata by HPLC-DAD-ESI-MS/MS

2014 ◽  
Vol 11 (1) ◽  
pp. 63-70 ◽  
Author(s):  
Jia-Yu ZHANG ◽  
Jian-Qiu LU ◽  
Xiao-Yan GAO ◽  
Qian ZHANG ◽  
Ning LI ◽  
...  
Keyword(s):  
Esi Ms ◽  
Murraya Paniculata

Biological activities of two polypore macrofungi (Basidiomycota) and characterization of their compounds using HPLC–DAD and LC–ESI–MS/MS

2021 ◽  
Author(s):  
Samaneh Chaharmiri Dokhaharani ◽  
Masoomeh Ghobad-Nejhad ◽  
Hamid Moghimi ◽  
Abbas Farazmand ◽  
Hossein Rahmani
Keyword(s):  
Biological Activities ◽  
Esi Ms

scholarly journals Proteomic Characterization of Bacteriophage Peptides from the Mastitis Producer Staphylococcus aureus by LC-ESI-MS/MS and the Bacteriophage Phylogenomic Analysis

Foods ◽  
2021 ◽  
Vol 10 (4) ◽  
pp. 799
Author(s):  
Ana G. Abril ◽  
Mónica Carrera ◽  
Karola Böhme ◽  
Jorge Barros-Velázquez ◽  
Benito Cañas ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Dairy Products ◽  
Phylogenomic Analysis ◽  
Esi Ms ◽  
Complement Inhibitors ◽  
Staphylococcus Spp ◽  
The Relationship ◽  
Phage Proteins ◽  
Identification And Characterization

The present work describes LC-ESI-MS/MS MS (liquid chromatography-electrospray ionization-tandem mass spectrometry) analyses of tryptic digestion peptides from phages that infect mastitis-causing Staphylococcus aureus isolated from dairy products. A total of 1933 nonredundant peptides belonging to 1282 proteins were identified and analyzed. Among them, 79 staphylococcal peptides from phages were confirmed. These peptides belong to proteins such as phage repressors, structural phage proteins, uncharacterized phage proteins and complement inhibitors. Moreover, eighteen of the phage origin peptides found were specific to S. aureus strains. These diagnostic peptides could be useful for the identification and characterization of S. aureus strains that cause mastitis. Furthermore, a study of bacteriophage phylogeny and the relationship among the identified phage peptides and the bacteria they infect was also performed. The results show the specific peptides that are present in closely related phages and the existing links between bacteriophage phylogeny and the respective Staphylococcus spp. infected.

Structural characterization of native and oxidized procyanidins (condensed tannins) from coffee pulp (Coffea arabica) using phloroglucinolysis and thioglycolysis-HPLC-ESI-MS

2021 ◽  
Vol 340 ◽  
pp. 127830
Author(s):  
Jorge E. Wong-Paz ◽  
Sylvain Guyot ◽  
Pedro Aguilar-Zárate ◽  
Diana B. Muñiz-Márquez ◽  
Juan C. Contreras-Esquivel ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Coffea Arabica ◽  
Condensed Tannins ◽  
Coffee Pulp ◽  
Esi Ms

scholarly journals Screening for the Optimal Specificity Profile of Protein Kinase C Using Electrospray Mass-Spectrometry

2005 ◽  
Vol 10 (4) ◽  
pp. 320-328 ◽  
Author(s):  
Mart Loog ◽  
Bo Ek ◽  
Nikita Oskolkov ◽  
Ale Närvänen ◽  
Jaak Järv ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase Activity ◽  
New Approach ◽  
Esi Ms ◽  
Kinase C ◽  
Kinase Specificity ◽  
Complex Structural ◽  
Novel Applications ◽  
Peptide Library Approach

A peptide library approach based on electrospray mass-spectrometric (ESI-MS) detection of phosphopeptides was designed for rapid and quantitative characterization of protein kinase specificity. The kcat/Km values for the protein kinase Cβ (PKCβ) were determined for a systematically varied set of individual substrate peptides in library mixtures by the ESI-MS method. The analysis revealed a complex structural specificity profile in positions around the phosphorylated serine with hydrophobic and/or basic residues being mostly preferred. On the basis of the kinetic parameters, a highly efficient peptide substrate for PKCβ (Kmvalue below 100 nM) FRRRRSFRRR and its alanine substituted pseudosubstrate-analog inhibitor (Ki value of 76 nM) were designed. The quantitative specificity profiles obtained by the new approach contained more information about kinase specificity than the conventional substrate consensus motifs. The new method presents a promising basis for design of substrate-site directed peptide or peptidomimetic inhibitors of protein kinases. Second, highly specific substrates could be designed for novel applications such as high-throughput protein kinase activity screens on protein kinase chips.

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