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ANALYSIS OF NON-ENZYMATIC POSTTRANSLATIONAL MODIFICATED (GLYCATED) ALBUMIN BY NANO-LC/MS/MS
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SYSNO ASEP 0436493 Druh ASEP C - Konferenční příspěvek (mezinárodní konf.) Zařazení RIV D - Článek ve sborníku Název ANALYSIS OF NON-ENZYMATIC POSTTRANSLATIONAL MODIFICATED (GLYCATED) ALBUMIN BY NANO-LC/MS/MS Tvůrce(i) Šťastná, Zdeňka (FGU-C)
Pataridis, Statis (FGU-C)
Sedláková, Pavla (FGU-C) RID
Mikšík, Ivan (FGU-C) RID, ORCID, SAIZdroj.dok. CECE 2012. 9th International Interdisciplinary Meeting on Bioanalysis. - Brno : Ústav analytické chemie AV ČR, v. v. i, 2012 / Foret František ; Křenková Jana ; Guttman Andras ; Klepárník Karel ; Boček Petr - ISBN 978-80-904959-1-3 Rozsah stran s. 61-65 Poč.str. 5 s. Forma vydání Tištěná - P Akce CECE 2012. International Interdisciplinary Meeting on Bioanalysis /9./ Datum konání 01.11.2012-02.11.2012 Místo konání Brno Země CZ - Česká republika Typ akce WRD Jazyk dok. eng - angličtina Země vyd. CZ - Česká republika Klíč. slova non-enzymatic glycation ; serum albumin Vědní obor RIV CB - Analytická chemie, separace CEP GAP206/12/0453 GA ČR - Grantová agentura ČR GA203/08/1428 GA ČR - Grantová agentura ČR Institucionální podpora FGU-C - RVO:67985823 UT WOS 000329635000014 Anotace Posttranslational modifications of proteins are important reactions, which significantly affect the function of proteins in the organism. In principle, they can be divided into enzymatic and non-enzymatic modifications. Non-enzymatic reactions include glycation (earlier called nonezymatic glycosylation), which plays an important role in the development of chronic complications of diabetes mellitus, uremia, in the process of aging and degeneration of the brain.This work deals with the study of glycated albumins (human serum albumin and bovine serum albumin). Methodologically we used nano-liquid chromatography coupled to Q-TOF mass spectrometer. In vitro modified proteins were cleavaged by trypsin and arising peptides were separated on C18 nano column with trap-column. Peptides and their modifications were analysed by high-resolution Q-TOF mass spectrometer MaXis with precision determination of mass below 2 ppm. We found some modifications of proteins. Besides well known carboxymethyllysine new ones were determined - create mass shift 78, 132 and 218. Origin of these modifications is discussed and possible structure is presented. All found modifications were allocated to the structure of proteins and reactivity to various oxo-compounds was also examined Pracoviště Fyziologický ústav Kontakt Lucie Trajhanová, lucie.trajhanova@fgu.cas.cz, Tel.: 241 062 400 Rok sběru 2015
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