Quaternized Trimethylaminated Polystyrene-Coated Zirconia as a Strong Anion Exchange Material for HPLC

2000 ◽  
Vol 72 (18) ◽  
pp. 4413-4419 ◽  
Author(s):  
Jianhong Zhao ◽  
Peter. W. Carr
Keyword(s):  
Anion Exchange ◽  
Strong Anion Exchange ◽  
Exchange Material

scholarly journals Extensive non-canonical phosphorylation in human cells revealed using strong-anion exchange-mediated phosphoproteomics

2017 ◽  
Author(s):  
Gemma Hardman ◽  
Simon Perkins ◽  
Zheng Ruan ◽  
Natarajan Kannan ◽  
Philip Brownridge ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Protein Phosphorylation ◽  
Anion Exchange ◽  
Human Cell ◽  
Cell Biology ◽  
Human Cells ◽  
Phosphopeptide Enrichment ◽  
Cell Extracts ◽  
Strong Anion Exchange ◽  
Acid Labile

Protein phosphorylation is a ubiquitous post-translational modification (PTM) that regulates all aspects of life. To date, investigation of human cell signalling has focussed on canonical phosphorylation of serine (Ser), threonine (Thr) and tyrosine (Tyr) residues. However, mounting evidence suggests that phosphorylation of histidine also plays a central role in regulating cell biology. Phosphoproteomics workflows rely on acidic conditions for phosphopeptide enrichment, which are incompatible with the analysis of acid-labile phosphorylation such as histidine. Consequently, the extent of non-canonical phosphorylation is likely to be under-estimated. We report an Unbiased Phosphopeptide enrichment strategy based on Strong Anion Exchange (SAX) chromatography (UPAX), which permits enrichment of acid-labile phosphopeptides for characterisation by mass spectrometry. Using this approach, we identify extensive and positional phosphorylation patterns on histidine, arginine, lysine, aspartate and glutamate in human cell extracts, including 310 phosphohistidine and >1000 phospholysine sites of protein modification. Remarkably, the extent of phosphorylation on individual non-canonical residues vastly exceeds that of basal phosphotyrosine. Our study reveals the previously unappreciated diversity of protein phosphorylation in human cells, and opens up avenues for exploring roles of acid-labile phosphorylation in any proteome using mass spectrometry.

scholarly journals Efficiency of crude corn extract clean-up on different columns in fumonisins determination

2005 ◽  
pp. 95-102 ◽  
Author(s):  
Biljana Abramovic ◽  
Sandra Jaksic ◽  
Zoran Masic
Keyword(s):  
Liquid Chromatography ◽  
Anion Exchange ◽  
Fluorescence Detection ◽  
Crude Extract ◽  
Reversed Phase ◽  
Lower Price ◽  
Strong Anion Exchange ◽  
Chromatographic Resolution ◽  
Immunoaffinity Columns ◽  
Fumonisins B1 And B2

The efficiencies of different clean-up procedures for crude corn extract from corn samples naturally contaminated by fumonisins B1 and B2 were compared. These procedures precede liquid chromatography determination with fluorescence detection. The efficiencies of immunoaffinity columns (IMA) strong anion exchange columns (SAX), as well as columns with reversed-phase C18 (RP C18) were investigated. No significant differences in the obtained results were found, regardless of the crude extract clea-nup procedure. However, the use of IMA columns for clean-up provided better chromatographic resolution, with the clean-up procedure being the simplest and the fastest. Also, because of the possibility of IMA column regeneration, it is possible to prepare ten samples on one column, so all in all, the lower price of SAX and RP C18 columns is of no great significance.

Analyses of Inositol Phosphates and by Strong Anion Exchange (SAX)-HPLC

2021 ◽  
pp. 365-378
Author(s):  
Debabrata Laha ◽  
Marília Kamleitner ◽  
Philipp Johnen ◽  
Gabriel Schaaf
Keyword(s):  
Anion Exchange ◽  
Inositol Phosphates ◽  
Strong Anion Exchange
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