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

Result code in 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>

Result on the web

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DOI - Digital Object Identifier

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Result language

angličtina

Original language name

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

Original language description

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

Czech name

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

Czech description

Byly studovány termostabilní deriváty trypsinu pro zdokonalené štěpení v gelu ve vysoce účinné proteomice.

Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CE - Biochemistry

OECD FORD branch

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Project

<a href="/en/project/ME%20664" target="_blank" >ME 664: Conjugates of proteolythic enzyms in highly outputable proteomic.</a><br>

Continuities

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

Publication year

2004

Confidentiality

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

Name of the periodical

Acta Universitatis Palackianae Olomucensis, Facultas Rerum Naturalium, Chemica

ISSN

0232-0061

e-ISSN

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Volume of the periodical

43

Issue of the periodical within the volume

S

Country of publishing house

CZ - CZECH REPUBLIC

Number of pages

275

Pages from-to

18-19

UT code for WoS article

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EID of the result in the Scopus database

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