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The chemical and enzymatic stability of the glycation products derived from opioid peptides (CROSBI ID 39718)

Prilog u knjizi | izvorni znanstveni rad

Jakas, Andreja ; Roščić, Maja ; Horvat, Štefica The chemical and enzymatic stability of the glycation products derived from opioid peptides // Peptides 2004 / Flegel, Martin ; Fridkin, Mati ; Gilon, Chaim et al. (ur.). Prag: Kenes Group, 2004. str. 589-590

Podaci o odgovornosti

Jakas, Andreja ; Roščić, Maja ; Horvat, Štefica

engleski

The chemical and enzymatic stability of the glycation products derived from opioid peptides

Nonenzymatic addition of reducing sugars such as glucose to the free amino groups of proteins, lipids or nucleic acid initiate complex reaction (Maillard reaction), leading at first to the formation of reversible glycated compounds having different structures. The following step is the formation of irreversibly bound, structurally heterogeneous products with covalent cross-linking properties. These adducts, called advanced glycation end products (AGEs) accumulate in long-lived proteins in vivo and account for complications in number of diseases such as diabetes, Alzheimers disease and aging itself. Herein we gave report on the stability of Amadori and imidazolidinone products as important link in the process of AGE products formation.

Maillard reaction, AGE products, Amadori compounds, imidazolidinone

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Podaci o prilogu

589-590.

objavljeno

Podaci o knjizi

Peptides 2004

Flegel, Martin ; Fridkin, Mati ; Gilon, Chaim ; Slaninova, Jirina

Prag: Kenes Group

2004.

965-90833-0-0

Povezanost rada

Kemija