scholarly journals Large-scale Analysis ofin VivoPhosphorylated Membrane Proteins by Immobilized Metal Ion Affinity Chromatography and Mass Spectrometry

2003 ◽  
Vol 2 (11) ◽  
pp. 1234-1243 ◽  
Author(s):  
Thomas S. Nühse ◽  
Allan Stensballe ◽  
Ole N. Jensen ◽  
Scott C. Peck
Keyword(s):  
Mass Spectrometry ◽  
Membrane Proteins ◽  
Affinity Chromatography ◽  
Metal Ion ◽  
Large Scale ◽  
Scale Analysis ◽  
Large Scale Analysis ◽  
Metal Ion Affinity Chromatography

scholarly journals Structural elucidation of triacylglycerol using online acetone Paternò–Büchi reaction coupled with reversed-phase liquid chromatography mass spectrometry

The Analyst ◽  
2020 ◽  
Vol 145 (20) ◽  
pp. 6532-6540 ◽  
Author(s):  
Elissia T. Franklin ◽  
Yu Xia
Keyword(s):  
Mass Spectrometry ◽  
Liquid Chromatography ◽  
Large Scale ◽  
Reversed Phase ◽  
Structural Elucidation ◽  
Scale Analysis ◽  
Liquid Chromatography Mass Spectrometry ◽  
Reversed Phase Liquid Chromatography ◽  
Large Scale Analysis ◽  
Phase Liquid

The developed online RPLC-PB-MS/MS system allows large scale analysis of isomeric triacylglycerol lipids differing in CC locations.

Clinical use of phosphorylated proteins in blood serum analysed by immobilised metal ion affinity chromatography and mass spectrometry

2012 ◽  
Vol 76 ◽  
pp. 36-42 ◽  
Author(s):  
Julian A.J. Jaros ◽  
Paul C. Guest ◽  
Hassan Ramoune ◽  
Matthias Rothermundt ◽  
F. Markus Leweke ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Affinity Chromatography ◽  
Blood Serum ◽  
Metal Ion ◽  
Clinical Use ◽  
Phosphorylated Proteins ◽  
Metal Ion Affinity Chromatography

scholarly journals Reliable identification of protein-protein interactions by crosslinking mass spectrometry

2020 ◽  
Author(s):  
Swantje Lenz ◽  
Ludwig R. Sinn ◽  
Francis J. O’Reilly ◽  
Lutz Fischer ◽  
Fritz Wegner ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Protein Interactions ◽  
Large Scale ◽  
Protein Complexes ◽  
Estimation Procedure ◽  
Scale Analysis ◽  
Protein Protein Interactions ◽  
False Discovery ◽  
Large Scale Analysis ◽  
False Discovery Rate Estimation

Crosslinking mass spectrometry is widening its scope from structural analyzes of purified multi-protein complexes towards systems-wide analyzes of protein-protein interactions. Assessing the error in these large datasets is currently a challenge. Using a controlled large-scale analysis of Escherichia coli cell lysate, we demonstrate a reliable false-discovery rate estimation procedure for protein-protein interactions identified by crosslinking mass spectrometry.

Understanding platelets

2005 ◽  
Vol 94 (11) ◽  
pp. 916-925 ◽  
Author(s):  
Marcus Dittrich ◽  
Ingvild Birschmann ◽  
Christiane Stuhlfelder ◽  
Albert Sickmann ◽  
Sabine Herterich ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Large Scale ◽  
Building Blocks ◽  
Clinical Implications ◽  
Scale Analysis ◽  
New Techniques ◽  
Analysis Techniques ◽  
Large Scale Analysis ◽  
Sage Data ◽  
New Framework

SummaryNew large-scale analysis techniques such as bioinformatics, mass spectrometry and SAGE data analysis will allow a new framework for understanding platelets. This review analyses some important options and tasks for these tools and examines an outline of the new, refined picture of the platelet outlined by these new techniques. Looking at the platelet-specific building blocks of genome, (active) transcriptome and proteome (notably secretome and phospho-proteome), we summarize current bioinformatical and biochemical approaches, tasks as well as their limitations. Understanding the surprisingly complex platelet regarding compartmentalization, key cascades, and pathways including clinical implications will remain an exciting and hopefully fruitful challenge for the future.

scholarly journals Zirconium(IV)-IMAC for phosphopeptide enrichment in phosphoproteomics

2020 ◽  
Author(s):  
Ignacio Arribas Diez ◽  
Ireshyn Govender ◽  
Previn Naicker ◽  
Stoyan Stoychev ◽  
Justin Jordaan ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Affinity Chromatography ◽  
Metal Ion ◽  
Large Scale ◽  
Cell Signalling ◽  
Phosphopeptide Enrichment ◽  
Magnetic Microparticles ◽  
Affinity Enrichment ◽  
Metal Oxide Affinity Chromatography ◽  
Enrichment Techniques

ABSTRACTPhosphopeptide enrichment is an essential step in large-scale, quantitative phosphoproteomics studies by mass spectrometry. Several phosphopeptide affinity enrichment techniques exist, such as Immobilized Metal ion Affinity Chromatography (IMAC) and Metal Oxide Affinity Chromatography (MOAC). We compared Zirconium (IV) IMAC (Zr-IMAC) magnetic microparticles to more commonly used Titanium (IV) IMAC (Ti-IMAC) and TiO2 magnetic microparticles for phosphopeptide enrichment from simple and complex protein samples prior phosphopeptide sequencing and characterization by mass spectrometry (LC-MS/MS). We optimized sample-loading conditions to increase phosphopeptide recovery for Zr-IMAC, Ti-IMAC and TiO2 based workflows. The performance of Zr-IMAC was enhanced by 19-22% to recover up to 5173 phosphopeptides from 200 µg of protein extract from HepG2/C3A cells, making Zr-IMAC the preferred method for phosphopeptide enrichment in this study. Ti-IMAC and TiO2 performance were also optimized to improve phosphopeptide numbers by 28% and 35%, respectively. Furthermore, Zr-IMAC based phosphoproteomics in the magnetic microsphere format identified 23% more phosphopeptides than HPLC-based Fe(III)-IMAC for same sample amount (200 µg), thereby adding 37% more uniquely identified phosphopeptides. We conclude that Zr-IMAC improves phosphoproteome coverage and recommend that this affinity enrichment method should be more widely used in biological and biomedical studies of cell signalling and in the search for disease-biomarkers.

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