Pseudotrypsin: a little known trypsin proteoform
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F18%3A73590131" target="_blank" >RIV/61989592:15310/18:73590131 - isvavai.cz</a>
Result on the web
<a href="https://www.mdpi.com/1420-3049/23/10/2637" target="_blank" >https://www.mdpi.com/1420-3049/23/10/2637</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.3390/molecules23102637" target="_blank" >10.3390/molecules23102637</a>
Alternative languages
Result language
angličtina
Original language name
Pseudotrypsin: a little known trypsin proteoform
Original language description
Trypsin is the protease of choice for protein sample digestion in proteomics. The most typical active forms are the single-chain beta-trypsin and the two-chain alfa-trypsin, which is produced by a limited autolysis of beta-trypsin. An additional intra-chain split leads to pseudotrypsin (psi-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, psi-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 psi-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), psi-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.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
<a href="/en/project/LO1204" target="_blank" >LO1204: Sustainable development of research in the Centre of the Region Haná</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2018
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
MOLECULES
ISSN
1420-3049
e-ISSN
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Volume of the periodical
23
Issue of the periodical within the volume
10
Country of publishing house
CH - SWITZERLAND
Number of pages
14
Pages from-to
"2637-1"-"2637-14"
UT code for WoS article
000451201400233
EID of the result in the Scopus database
2-s2.0-85054848644