Evaluation of pseudotrypsin cleavage specificity towards proteins by MALDI-TOF mass spectrometry

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F15%3A33156813" target="_blank" >RIV/61989592:15310/15:33156813 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60162694:G44__/15:43875471

Výsledek na webu

<a href="http://dx.doi.org/10.2174/0929866522666151008151617" target="_blank" >http://dx.doi.org/10.2174/0929866522666151008151617</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.2174/0929866522666151008151617" target="_blank" >10.2174/0929866522666151008151617</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Evaluation of pseudotrypsin cleavage specificity towards proteins by MALDI-TOF mass spectrometry

Popis výsledku v původním jazyce

Trypsin is a protease, which is commonly used for the digestion of protein samples in proteomic experiments. The process of trypsin autolysis is known to produce autolytic peptides as well as active enzyme forms with one or more intra-chain splits. In consequence, their variable presence can influence the digestion of a protein substrate in the reaction mixture. Besides two major and well-studied forms named beta-trypsin and alpha-trypsin, there are also other active trypsin forms known such as gamma-trypsin and pseudotrypsin (psi-trypsin). In this work, the cleavage specificity of psi-trypsin was evaluated using in-gel digestion of protein standards followed by matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry (MS) and tandem mass spectrometry (MS/MS) analyses of the resulting peptides. The numbers of produced and matching peptides were similar to those obtained using alpha-/beta-trypsin. The same experience was obtained with a real complex prote

Název v anglickém jazyce

Evaluation of pseudotrypsin cleavage specificity towards proteins by MALDI-TOF mass spectrometry

Popis výsledku anglicky

Trypsin is a protease, which is commonly used for the digestion of protein samples in proteomic experiments. The process of trypsin autolysis is known to produce autolytic peptides as well as active enzyme forms with one or more intra-chain splits. In consequence, their variable presence can influence the digestion of a protein substrate in the reaction mixture. Besides two major and well-studied forms named beta-trypsin and alpha-trypsin, there are also other active trypsin forms known such as gamma-trypsin and pseudotrypsin (psi-trypsin). In this work, the cleavage specificity of psi-trypsin was evaluated using in-gel digestion of protein standards followed by matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry (MS) and tandem mass spectrometry (MS/MS) analyses of the resulting peptides. The numbers of produced and matching peptides were similar to those obtained using alpha-/beta-trypsin. The same experience was obtained with a real complex prote

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2015

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Protein and Peptide Letters

ISSN

0929-8665

e-ISSN

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Svazek periodika

22

Číslo periodika v rámci svazku

12

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

10

Strana od-do

1123-1132

Kód UT WoS článku

000365041200011

EID výsledku v databázi Scopus

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