Inaktivace aspartát aminostransferázy vyvolaná glykací. Vliv kyseliny močové
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11150%2F05%3A00004765" target="_blank" >RIV/00216208:11150/05:00004765 - isvavai.cz</a>
Nalezeny alternativní kódy
RIV/00216208:11160/05:00007093
Výsledek na webu
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DOI - Digital Object Identifier
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Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Glycation-Induced Inactivation of Aspartate Aminotransferase, Effect of Uric Acid
Popis výsledku v původním jazyce
Glycation is common posttranslational modification of proteins impairing their function, which occurs during diabetes mellitus and aging.Beside extracellular glycation of long-lived proteins, intracellular modifications of short-lived proteins by more reactive sugars like fructose are possible.The process includes free oxygen radicals (glycoxidation).In an attempt to reduce glycoxidation and formation of advanced glycation products, influence of 0.2-1.2 mM uric acid as endogenous antioxidant on glycoxidation of purified pig heart aspartate aminotransferase (AST) by 50 mM and 500 mM D-fructose in vitro was studied.Uric acid at 1.2 mM concentration reduced AST activity decrease and formation of total AGE products caused by incubation in vitro of the enzyme with sugar up to 25 days at 37 °C.The results thus support the hypothesis that uric acid has beneficial effects in controlling protein glycoxidation.The in vitro system AST-fructose proved to be a useful tool for investigation of glyca
Název v anglickém jazyce
Glycation-Induced Inactivation of Aspartate Aminotransferase, Effect of Uric Acid
Popis výsledku anglicky
Glycation is common posttranslational modification of proteins impairing their function, which occurs during diabetes mellitus and aging.Beside extracellular glycation of long-lived proteins, intracellular modifications of short-lived proteins by more reactive sugars like fructose are possible.The process includes free oxygen radicals (glycoxidation).In an attempt to reduce glycoxidation and formation of advanced glycation products, influence of 0.2-1.2 mM uric acid as endogenous antioxidant on glycoxidation of purified pig heart aspartate aminotransferase (AST) by 50 mM and 500 mM D-fructose in vitro was studied.Uric acid at 1.2 mM concentration reduced AST activity decrease and formation of total AGE products caused by incubation in vitro of the enzyme with sugar up to 25 days at 37 °C.The results thus support the hypothesis that uric acid has beneficial effects in controlling protein glycoxidation.The in vitro system AST-fructose proved to be a useful tool for investigation of glyca
Klasifikace
Druh
J<sub>x</sub> - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)
CEP obor
CE - Biochemie
OECD FORD obor
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Návaznosti výsledku
Projekt
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Návaznosti
S - Specificky vyzkum na vysokych skolach
Ostatní
Rok uplatnění
2005
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Molecular and Cellular Biochemistry
ISSN
0300-8177
e-ISSN
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Svazek periodika
278
Číslo periodika v rámci svazku
1-2
Stát vydavatele periodika
NL - Nizozemsko
Počet stran výsledku
8
Strana od-do
85-92
Kód UT WoS článku
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EID výsledku v databázi Scopus
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