The glycosylated hemoglobin in the blood reacts with the blood sugar level in organisms for a period of time, which has been used as an important index for the diagnosis and treatment of diabetes in recent years. At present, enzymatic method is mainly used to detect the content of glycosylated hemoglobin in human body. A special kind of enzymes, fructose valine oxidase, is used to determine the content of glycosylated hemoglobin. The enzyme acts on glycosylated polypeptide or glycosylated amino acid. Its products undergo a series of redox reactions. Finally, the content of glycosylated hemoglobin is determined by the color of the end product. 。 Therefore, fructose valine oxidase is the key enzyme in the determination of glycosylated hemoglobin.
Current studies have shown that the glycosylation site of glycosylated hemoglobin in human blood is valine-NH2 residue, so the preparation of a simulated substrate of glycosylated hemoglobin in human blood, namely fructose-valine [N-(1-deoxy-D-fructose-1-yl) -valine], is particularly important for screening high activity, high stability and high specificity of fructose-valine oxidase and studying its enzymatic properties.
CAS No. 10003-64-2
Molecular formula: C11H21NO7
Relative molecular mass: 279.29
Preservation conditions: long-term preservation at 2-8 C; separate water after dissolution according to dosage and freeze at - 20 C to avoid repeated freezing and thawing as far as possible.
Instructions: Fructose valine oxidase catalyzes the reaction of fructose valine to produce hydrogen peroxide. Hydrogen peroxide reacts with 4-aminoantipyridine and TBHB under the action of peroxidase.
Safety tips: This reagent is only used for research and development or production, and is strictly prohibited for human or animal experiments.
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