GOLD

Nombre químico: Glyoxyl-derived lysine dimer acetic acid salt // Sinónimos: 1,3-bis((S)-5-amino-5-carboxypentyl)-1H-imidazol-3-ium acetic acid salt

  • Nº Artículo:HAA3070
  • Nº CAS:209267-39-0
  • Fórmula:C15H27N4O4
  • Storage temperature:-20°C
  • Masa molecular:327,40 g/mol

from 165,00 €

Grouped product items
Cantidad Unidad de venta Precio Unidad de almacenamiento de stock (SKU) Disponibilidad
10 mg
165,00 €
HAA3070.0010
<10 días laborables
Hoja de seguridad
description

Maillard Reaction Products (MRPs) are indicators for the heat treatment of food, as well as markers of nutritional quality. They also appear naturally in the human body as so-called Advanced Glycation End Products (AGEs). As such, they are indicators for body health and disease processes, including inflammation, diabetes, cancer and ageing. Consequently, AGEs gained broad attention in cosmetics, biochemistry, food, and pharmaceutical applications.

This material is supplied as a salt containing varying contents of the acid counterion. The net content of each batch is specified in the respective certificate of analysis.


references

Intact glycation end products containing carboxymethyl-lysine and glyoxal lysine dimer obtained from synthetic collagen model peptide; H. Yamada, T. Sasaki, S. Niwa, T. Oishi, M. Murata, T. Kawakami and S. Aimoto; Bioorg Med Chem Lett 2004; 14: 5677-80. https://doi.org/10.1016/j.bmcl.2004.08.044

Protein crosslinking by the Maillard reaction: dicarbonyl-derived imidazolium crosslinks in aging and diabetes; P. Chellan and R. H. Nagaraj; Archives of biochemistry and biophysics 1999; 368: 98-104. https://doi.org/10.1006/abbi.1999.1291

Role of the Maillard reaction in aging of tissue proteins. Advanced glycation end product-dependent increase in imidazolium cross-links in human lens proteins; E. B. Frye, T. P. Degenhardt, S. R. Thorpe and J. W. Baynes; J Biol Chem 1998; 273: 18714-9. https://doi.org/10.1074/jbc.273.30.18714

Imidazolium crosslinks derived from reaction of lysine with glyoxal and methylglyoxal are increased in serum proteins of uremic patients: evidence for increased oxidative stress in uremia; H. Odani, T. Shinzato, J. Usami, Y. Matsumoto, E. Brinkmann Frye, J. W. Baynes and K. Maeda; FEBS Lett 1998; 427: 381-5. https://doi.org/10.1016/s0014-5793(98)00416-5

Characterization of an Imidazolium Salt Formed from Glyoxal and N.alpha.-Hippuryllysine: A Model for Maillard Reaction Crosslinks in Proteins; K. J. Wells-Knecht, E. Brinkmann and J. W. Baynes; The Journal of Organic Chemistry 1995; 60: 6246-6247. https://doi.org/10.1021/jo00125a001



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