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Original title:
ANALYSIS OF NON-ENZYMATIC POSTTRANSLATIONAL MODIFICATED (GLYCATED) ALBUMIN BY NANO-LC/MS/MS
Authors: Šťastná, Zdeňka ; Pataridis, Statis ; Sedláková, Pavla ; Mikšík, Ivan
Document type: Papers
Conference/Event: CECE 2012. International Interdisciplinary Meeting on Bioanalysis /9./, Brno (CZ), 2012-11-01 / 2012-11-02
Year: 2012
Language: eng
Abstract: 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
Keywords: non-enzymatic glycation; serum albumin
Project no.: GAP206/12/0453 (CEP), GA203/08/1428 (CEP)
Funding provider: GA ČR, GA ČR
Host item entry: CECE 2012. 9th International Interdisciplinary Meeting on Bioanalysis, ISBN 978-80-904959-1-3
Institution: Institute of Physiology AS ČR (web)
Document availability information: Fulltext is available at the institute of the Academy of Sciences.
Original record: http://hdl.handle.net/11104/0240234
Permalink: http://www.nusl.cz/ntk/nusl-178145
The record appears in these collections:
Research > Institutes ASCR > Institute of Physiology
Conference materials > Papers
Authors: Šťastná, Zdeňka ; Pataridis, Statis ; Sedláková, Pavla ; Mikšík, Ivan
Document type: Papers
Conference/Event: CECE 2012. International Interdisciplinary Meeting on Bioanalysis /9./, Brno (CZ), 2012-11-01 / 2012-11-02
Year: 2012
Language: eng
Abstract: 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
Keywords: non-enzymatic glycation; serum albumin
Project no.: GAP206/12/0453 (CEP), GA203/08/1428 (CEP)
Funding provider: GA ČR, GA ČR
Host item entry: CECE 2012. 9th International Interdisciplinary Meeting on Bioanalysis, ISBN 978-80-904959-1-3
Institution: Institute of Physiology AS ČR (web)
Document availability information: Fulltext is available at the institute of the Academy of Sciences.
Original record: http://hdl.handle.net/11104/0240234
Permalink: http://www.nusl.cz/ntk/nusl-178145
The record appears in these collections:
Research > Institutes ASCR > Institute of Physiology
Conference materials > Papers
Record created 2014-12-11, last modified 2021-11-24