Sort   by:  
 Page size 
ProteomicsThe fate of bioaccessible coeliac toxic motifs and IgE epitopes during simulated gastro-intestinal digestion of pizza base
Understanding how food processing may modify allergen bioaccessibility and the evolution of immunologically active peptides in the gastrointestinal tract is essential if knowledge-based ap-proaches to reducing the allergenicity of food is to be realised. A soy-enriched wheat-based pizza base was sub...
ORGANISM(S): Glycine max Triticum aestivum (Wheat) 
2022-08-12 | PXD031067 | Pride
Allergen In vitro digestion Ige epitope Allergenicity risk assessment. Coeliac toxic motif Wheat Soy Gluten Mass spectrome-try 
UnknownThe Fate of IgE Epitopes and Coeliac Toxic Motifs during Simulated Gastrointestinal Digestion of Pizza Base.
Not available
S-EPMC9318710 | biostudies-literature
ProteomicsPeptide profile of the storage proteins of chickpea, wheat, soybean analyzed with LC-MS/MS
Aiming to reduce food spoilage, the present study developed novel highly active food-grade preservatives affecting a wide range of bacteria. For this purpose, storage proteins were extracted from food plants. After enzymatic hydrolysis by the digestive protease chymotrypsin, the peptide profiles wer...
ORGANISM(S): Cicer arietinum (Chickpea) (Garbanzo) Glycine max Triticum aestivum (Wheat) 
2021-01-11 | PXD019257 | Pride
Storage proteins Chickpea Chymotryptic digestion Soybean Wheat Lc-ms/ms 
ProteomicsSite-specific glycosylation of donkey milk lactoferrin investigated by High Resolution Mass Spectrometry
A comprehensive glycosylation profile of donkey lactoferrin, isolated by ion exchange chromatography from an individual milk sample, was obtained by means of chymotryptic digestion, TiO2 and HILIC enrichment, reversed-phase high performance liquid chromatography, electrospray mass spectrometry, and...
ORGANISM(S): Equus asinus (Donkey) 
2016-08-25 | PXD004289 | Pride
Lactoferrin glycosylation · donkey milk · n-glycan structures · tio2 and hilic enrichment · mass spectrometry 
UnknownDetecting Differences in Prion Protein Conformation by Quantifying Methionine Oxidation.
Not available
S-EPMC8793083 | biostudies-literature
ProteomicsEnhanced Proteomics Analysis with a Novel Recombinant Chymotrypsin Analogue En-gineered for High Cleavage Specificity
Chymotrypsin is widely used in shotgun proteomics owing to its orthogonal cleavage specificity relative to trypsin, which enhances sequence coverage of hydrophobic protein regions. However, commercial preparations often display variable cleavage specificity, trypsin contamination, and elevated misse...
ORGANISM(S): Homo sapiens (Human) 
2026-06-08 | PXD072165 | Pride
Chymotrypsin Missed cleavages Sample preparation Proteomics Protein digestion 
ProteomicsGel-free mass spectrometry analysis of Drosophila melanogaster heads
Here we describe a bottom-up approach to analyse an enriched membrane fraction from Drosophila melanogaster heads using multidimensional liquid chromatography (LC) coupled with tandem-mass spectrometry (MS/MS) that relies on a complete solubilisation and digestion of proteins. An enriched membrane f...
ORGANISM(S): Drosophila melanogaster (Fruit fly) 
2015-07-27 | PXD001712 | Pride
Proteomics Mass spectrometry Heads Membrane proteins Drosophila melanogaster 
ProteomicsCharacterisation of the transcriptome and proteome of SARS-CoV-2 using direct RNA sequencing and tandem mass spectrometry reveals evidence for a cell passage induced in-frame deletion in the spike glycoprotein that removes the furin-like cleavage site.
Direct RNA sequencing using an Oxford Nanopore MinION characterised the transcriptome of SARS-CoV-2 grown in Vero E6 cells. This cell line is being widely used to propagate the novel coronavirus. The viral transcriptome was analysed using a recently developed ORF-centric pipeline. This revealed the ...
ORGANISM(S): Chlorocebus sabaeus 
2020-03-31 | PXD018241 | Pride
Human Multiomics Coronavirus Sars-cov-2 
ProteomicsProteomic Analysis of Oil-Roasted Cashew Using a Customized Database
Cashew is one of the most prevalent causes of tree nut allergies. However, the cashew proteome is far from complete, which limits the quality of peptide identification in mass spectrometric analyses. In this study, bioinformatics tools were utilized to construct a customized cashew protein database ...
ORGANISM(S): Anacardium occidentale 
2022-06-07 | PXD027543 | Pride
Cashew Proteogenomics Allergen Proteomics Oil roasting 
UnknownEnhanced trypsin on a budget: Stabilization, purification and high-temperature application of inexpensive commercial trypsin for proteomics applications.
Not available
S-EPMC6597055 | biostudies-literature
Sort   by:  
 Page size