Enzymové a lektinové magnetické reaktory pro analýzu glykoproteinů

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216275%3A25310%2F05%3A00003013" target="_blank" >RIV/00216275:25310/05:00003013 - 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

Enzyme and Lectin Magnetic Reactors for Analysis of Glycoproteins by Signature Peptide Approach

Popis výsledku v původním jazyce

For qualitative identification and characterization of proteins with high heterogeneity in post-translational modification and amino acid composition the signature peptides approach is preferable to peptide mapping technique. In order to develop improvedmethod for determination of agalactosylated form of model glycoprotein immunoglobulin G which is closely associated with autoimmune diseases, we decided to combine the high specificity of enzyme and lectin magnetic reactors with sensitivity of MS analysis. Due to the high variability of amino-acid compositions and the present of additional four potential glycosylation sites in the hypervariable regions of Fab fragment, IgG molecules had to be splitted using papain reactor and obtained Fc fragments wereafter purified by affinity chromatography. The signature peptides of IgG are derived from Fc-fragments with conserved N-glycosylation site at the position Asn297.Highly active enzyme reactors with immobilized TPCK-trypsin, neuraminidase,

Název v anglickém jazyce

Enzyme and Lectin Magnetic Reactors for Analysis of Glycoproteins by Signature Peptide Approach

Popis výsledku anglicky

For qualitative identification and characterization of proteins with high heterogeneity in post-translational modification and amino acid composition the signature peptides approach is preferable to peptide mapping technique. In order to develop improvedmethod for determination of agalactosylated form of model glycoprotein immunoglobulin G which is closely associated with autoimmune diseases, we decided to combine the high specificity of enzyme and lectin magnetic reactors with sensitivity of MS analysis. Due to the high variability of amino-acid compositions and the present of additional four potential glycosylation sites in the hypervariable regions of Fab fragment, IgG molecules had to be splitted using papain reactor and obtained Fc fragments wereafter purified by affinity chromatography. The signature peptides of IgG are derived from Fc-fragments with conserved N-glycosylation site at the position Asn297.Highly active enzyme reactors with immobilized TPCK-trypsin, neuraminidase,

Druh

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

CEP obor

CB - Analytická chemie, separace

OECD FORD obor

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Projekt

<a href="/cs/project/GA203%2F02%2F0023" target="_blank" >GA203/02/0023: Vývoj nových postupů pro vysoce spolehlivou analyt. kontrolu technol.,materiálů,potravin a život. prostř. a pro lékařskou diag. s využitím moderní instrumentace</a><br>

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2005

Kód důvěrnosti údajů

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

Název periodika

Scientific Papers of the University of Pardubice, Series A

ISSN

1211-5541

e-ISSN

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Svazek periodika

11

Číslo periodika v rámci svazku

neuveden

Stát vydavatele periodika

CZ - Česká republika

Počet stran výsledku

17

Strana od-do

15-31

Kód UT WoS článku

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EID výsledku v databázi Scopus

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