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Screening for glucose-triggered modifications of glutathione (CROSBI ID 149949)

Prilog u časopisu | izvorni znanstveni rad | međunarodna recenzija

Jerić, Ivanka ; Horvat, Štefica Screening for glucose-triggered modifications of glutathione // Journal of peptide science, 15 (2009), 8; 540-547. doi: 10.1002/psc.1159

Podaci o odgovornosti

Jerić, Ivanka ; Horvat, Štefica

engleski

Screening for glucose-triggered modifications of glutathione

Nonenzymatic protein glycation is caused by a Schiff's base reaction between the aldehyde groups of reducing sugars and the primary amines of proteins. These structures may undergo further Amadori rearrangement and free radical-mediated oxidation to finally generate irreversible advanced glycation end products (AGEs). One of the factors known to modulate the glycation of proteins is glutathione, the most abundant nonprotein thiol tripeptide with the  -linkage, H-Glu(Cys-Gly-OH)-OH (GSH). Screening for products formed by GSH with D-glucose is an essential step in understanding the participation of GSH in glycation (the Maillard) reaction. Under the conditions used in these studies we observed N-(1-deoxy-D-fructos-1-yl)-pyroglutamic acid as the major glycation product formed in the mixtures of GSH and glucose in vitro. A reversed-phase HPLC/MS and tandem mass spectrometry analyses of the GSH/glucose mixtures revealed that cleavage of the N-terminal glutamic acid and the formation of pyroglutamic acid-related Amadori product was accompanied by Cys-Gly-derived Amadori and thiazolidine compounds.

glutathione ; glycation ; Amadori ; thiazolidine ; mass spectrometry ; Maillard

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Podaci o izdanju

15 (8)

2009.

540-547

objavljeno

1075-2617

1099-1387

10.1002/psc.1159

Povezanost rada

Kemija

Poveznice
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