ReviewMolecules (Basel, Switzerland)2018
Pseudotrypsin: A Little-Known Trypsin Proteoform.
Review in Molecules (Basel, Switzerland), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Effects of Polypropylene and Polyethylene Terephthalate Microplastics on Trypsin Structure and Function.International journal of molecular sciences · 2025Article
- Analysis of Protein Inhibitors of Trypsin in Quinoa, Amaranth and Lupine Seeds. Selection and Deep Structure-Function Characterization of theInternational journal of molecular sciences · 2025Article
- Clean and Complete Protein Digestion with an Autolysis Resistant Trypsin for Peptide Mapping.Journal of proteome research · 2024Article
- Quenching Trypsin Is Unnecessary in Filter-Based Bottom-Up Proteomics.Journal of the American Society for Mass Spectrometry · 2024Article
- Optimal conditions for carrying out trypsin digestions on complex proteomes: From bulk samples to single cells.Journal of proteomics · 2024Review
- Bioassay-Guided Alkaloids Isolation fromMolecules (Basel, Switzerland) · 2023Article
- Detergent-Assisted Protein Digestion-On the Way to Avoid the Key Bottleneck of Shotgun Bottom-Up Proteomics.International journal of molecular sciences · 2022Review
- SPACEPro: A Software Tool for Analysis of Protein Sample Cleavage for Tandem Mass Spectrometry.Journal of proteome research · 2021Article
- Article
- Deviation of Trypsin Activity Using Peptide Conformational Imprints.Nanomaterials (Basel, Switzerland) · 2021Article
- Review
- Nonspecific cleavages arising from reconstitution of trypsin under mildly acidic conditions.PloS one · 2020Article
- Special Issue: Mass Spectrometric Proteomics.Molecules (Basel, Switzerland) · 2019Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Trypsin is the protease of choice for protein sample digestion in proteomics. The most typical active forms are the single-chain β-trypsin and the two-chain α-trypsin, which is produced by a limited autolysis of β-trypsin. An additional intra-chain split leads to pseudotrypsin (ψ-trypsin) with three chains interconnected by disulfide bonds, which can be isolated from the autolyzate by ion-exchange chromatography. Based on experimental data with artificial substrates, peptides, and protein standards, ψ-trypsin shows altered kinetic properties, thermodynamic stability and cleavage site preference (and partly also cleavage specificity) compared to the above-mentioned proteoforms. In our laboratory, we have analyzed the performance of bovine ψ-trypsin in the digestion of protein samples with a different complexity. It cleaves predominantly at the characteristic trypsin cleavage sites. However, in a comparison with common tryptic digestion, non-specific cleavages occur more frequently (mostly after the aromatic residues of Tyr and Phe) and more missed cleavages are generated. Because of the preferential cleavages after the basic residues and more developed side specificity, which is not expected to occur for the major trypsin forms (but may appear anyway because of their autolysis), ψ-trypsin produces valuable information, which is complementary in part to data based on a strictly specific trypsin digestion and thus can be unnoticed following common proteomics protocols.
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Registered trials
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