Termostabilní deriváty trypsinu pro zdokonalené štěpení v gelu ve vysoce účinné proteomice

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F04%3A00002285" target="_blank" >RIV/61989592:15310/04:00002285 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Thermostable trypsin derivatives for enhanced in-gel digestion in high throughput proteomics

Popis výsledku v původním jazyce

Proteomics is the emerging scientific discipline focused on understanding of molecular processes in the cell through a large-scale study of proteins existing in a specific biological context (proteome). Identification of proteins after electrophoretic separations in polyacrylamide gels is typically achieved by their enzymatic in-gel digestion and analyzing the recovered peptides by mass spectrometry. However, a poor yield of the digestion products has been recognized as a serious bottleneck in further progress in high throughput proteomics. Hence accelerated digestion of protein would represent a major advance towards the cost-effective #real-time# flexible characterization of proteomes. Here we report a study on development of autolysis-resistant bovine trypsin (BT) conjugates showing high catalytic activity at elevated temperatures. BT was modified by coupling of various sugars or sugar-moiety-containing compounds to primary amino groups (lysine residues) in the enzyme molecule. For

Název v anglickém jazyce

Thermostable trypsin derivatives for enhanced in-gel digestion in high throughput proteomics

Popis výsledku anglicky

Proteomics is the emerging scientific discipline focused on understanding of molecular processes in the cell through a large-scale study of proteins existing in a specific biological context (proteome). Identification of proteins after electrophoretic separations in polyacrylamide gels is typically achieved by their enzymatic in-gel digestion and analyzing the recovered peptides by mass spectrometry. However, a poor yield of the digestion products has been recognized as a serious bottleneck in further progress in high throughput proteomics. Hence accelerated digestion of protein would represent a major advance towards the cost-effective #real-time# flexible characterization of proteomes. Here we report a study on development of autolysis-resistant bovine trypsin (BT) conjugates showing high catalytic activity at elevated temperatures. BT was modified by coupling of various sugars or sugar-moiety-containing compounds to primary amino groups (lysine residues) in the enzyme molecule. For

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/ME%20664" target="_blank" >ME 664: Konjugáty proteolytických enzymů ve vysoce výkonné proteomice</a><br>

Návaznosti

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

Rok uplatnění

2004

Kód důvěrnosti údajů

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

Název periodika

Acta Universitatis Palackianae Olomucensis, Facultas Rerum Naturalium, Chemica

ISSN

0232-0061

e-ISSN

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Svazek periodika

43

Číslo periodika v rámci svazku

S

Stát vydavatele periodika

CZ - Česká republika

Počet stran výsledku

275

Strana od-do

18-19

Kód UT WoS článku

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EID výsledku v databázi Scopus

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