ArticleJournal of the American Society for Mass Spectrometry2010
Investigating alternative acidic proteases for H/D exchange coupled to mass spectrometry: plasmepsin 2 but not plasmepsin 4 is active under quenching conditions.
Article in Journal of the American Society for Mass Spectrometry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed.
- Selenized Chickpea Sprouts Hydrolysates as a Potential Anti-Aging Ingredient.Molecules (Basel, Switzerland) · 2023Article
- Hydrogen/Deuterium Exchange Mass Spectrometry of Heme-Based Oxygen Sensor Proteins.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Article
- High-Resolution HDX-MS of Cytochrome c Using Pepsin/Fungal Protease Type XIII Mixed Bed Column.Journal of the American Society for Mass Spectrometry · 2019Article
- Down-regulation of NOX2 activity in phagocytes mediated by ATM-kinase dependent phosphorylation.Free radical biology & medicine · 2017Article
- Analytical Aspects of Hydrogen Exchange Mass Spectrometry.Annual review of analytical chemistry (Palo Alto, Calif.) · 2015Review
- Accessing the reproducibility and specificity of pepsin and other aspartic proteases.Biochimica et biophysica acta · 2013Article
- Nepenthesin from monkey cups for hydrogen/deuterium exchange mass spectrometry.Molecular & cellular proteomics : MCP · 2013Article
- Hydrogen exchange mass spectrometry: are we out of the quicksand?Journal of the American Society for Mass Spectrometry · 2012Review
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Structural studies of proteins by hydrogen/deuterium exchange coupled to mass spectrometry (DXMS) require the use of proteases working at acidic pH and low temperatures. The spatial resolution of this technique can be improved by combining several acidic proteases, each generating a set of different peptides. Three commercial aspartic proteases are used, namely, pepsin, and proteases XIII and XVIII. However, given their low purity, high enzyme/protein ratios have to be used with proteases XIII and XVIII. In the present work, we investigate the activity of two alternative acidic proteases from Plasmodium falciparum under different pH and temperature conditions. Peptide mapping of four different proteins after digestion with pepsin, plasmepsin 2 (PSM2), and plasmepsin 4 (PSM4) were compared. PSM4 is inactive at pH 2.2 and 0 degrees C, making it unusable for DXMS studies. However, PSM2 showed low but reproducible activity under DXMS conditions. It displayed no substrate specificity and, like pepsin, no strict sequence specificity. Altogether, these results show that PSM2 but not PSM4 is a potential new tool for DXMS studies.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.