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L–α–Glycerophosphate Oxidase (GPO)
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  • Übersicht

    Beschreibung

    L–α–Glycerophosphate Oxidase (GPO) is a flavin-dependent enzyme that catalyzes the oxidation of sn-glycerol-3-phosphate to dihydroxyacetone phosphate (DHAP), with the production of hydrogen peroxide (H₂O₂) as a byproduct. This reaction plays an essential role in glycerol metabolism, serving as a critical link between lipid catabolism, glycolysis, and lipid biosynthesis through the generation of DHAP—a central intermediate in energy and metabolic pathways. In clinical and biochemical applications, GPO is frequently used in enzymatic assays for the quantification of triglycerides and glycerol. The hydrogen peroxide produced is coupled with a colorimetric reaction, allowing for easy detection and measurement. Due to its specificity and efficiency, GPO plays a vital role in analytical biochemistry and is a useful tool in both clinical laboratories and metabolic research.

  • Spezifikationen

    • Expressionssystem

      Escherichia coli

      Detektionsmethode

      Spectrophotometry

    • Konzentration

      10 U/mg or more

      Aktivität

      Activity can be calculated by using the following formula:
      Volume activity (U/ mL)＝ ΔOD/ min (ΔOD test−ΔOD blank) × Vt × 2 × df /(13.2×1.0×Vs)
      ＝ ΔOD/ min × 4.696 × df
      Weight activity (U/mg)＝ (U/mL)×1/C
      Vt: Total volume (1.55 mL)
      Vs: Sample volume (0.05 mL)
      13.2: Millimolar absorption coefficient of quinoneimine dye
      2: Conversion factor (one mole of quinoneimine dye corresponds to two moles of glycerophophate)
      1.0: Light path length (cm)
      df: Dilution factor
      C: Enzyme concentration in dissolution (mg/mL)

    • Einheitsdefinition

      One unit is defined as the enzyme quantity which oxidizes one micromole of L-α-Glycerol-phosphate per minute under the following conditions: 84 mM Potassium phosphate, 425 mM L-α-Glycerol-phosphate, 0.03% 4-Aminoantipyrine, 0.024% Phenol, and 1.9 U/mL Peroxidase.

      Reaktionsbedingung

      84 mM Potassium phosphate, 425 mM L-α-Glycerol-phosphate, 0.03% 4-Aminoantipyrine, 0.024% Phenol, and 1.9 U/mL Peroxidase

    • Form

      Lyophilized

  • Hintergrund

    • Synonyme

      GPO, Glycerol phosphate oxidase, α-Glycerophosphate oxidase, L–α–Glycerol-3-phosphate oxidase, G3P oxidase, Flavin-dependent oxidase, FAD oxidoreductase, Glycerophosphate:oxygen oxidoreductase, L–α–Glycerophosphate:oxygen oxidoreductase, Glycerol phosphate oxygenase, Aerococcus oxidase, Corynebacterium glycerophosphate oxidase, EC 1.1.3.21 enzyme

  • Anleitung

    • Rekonstitution

      It is recommended to weigh and reconstitute 10 mg of lyophilized powder in 125 μL double-distilled water directly and incubate the solution for at least 10 mins to ensure sufficient re-dissolved.

      Versand

      The product is shipped with polar packs. Upon receipt, store it immediately at -20°C or lower for long term storage.

    • Stabilität & Lagerung

      This product is stable at -20°C for long-term storage under sterile conditions.
      Avoid repeated free-thaw cycles.

  • Bild
    The effects of various chemicals on GPO. The enzyme was incubated with the chemicals at 25°C for 1 hour

    The effects of various chemicals on GPO.
    The enzyme was incubated with the chemicals at 25°C for 1 hour

    pH stability of GPO. The enzyme powder was reconstituted by double-distilled water and treated with different pH buffer condition for 20 hours. pH 4.0-6.0, 0.1 M Sodium citrate buffer; pH 7.0-8.0, 0.1 M Potassium phosphate buffer; pH 8.5, 0.1 M Tris-HCl buffer; pH 10.0-11.0, 0.1 M Carbonate-bicarbonate buffer.

    pH stability of GPO.
    The enzyme powder was reconstituted by double-distilled water and treated with different pH buffer condition for 20 hours. pH 4.0-6.0, 0.1 M Sodium citrate buffer; pH 7.0-8.0, 0.1 M Potassium phosphate buffer; pH 8.5, 0.1 M Tris-HCl buffer; pH 10.0-11.0, 0.1 M Carbonate-bicarbonate buffer.

    Thermal stability of GPO. The enzyme powder was reconstituted by double-distilled water and treated with different temperatures for 15 minutes. Final concentration: 21.6 U/ mL.

    Thermal stability of GPO.
    The enzyme powder was reconstituted by double-distilled water and treated with different temperatures for 15 minutes. Final concentration: 21.6 U/ mL.

    pH activity of GPO. The buffer conditions with various pH values were used in the reaction at 37°C. pH 4.0-6.0, 0.1 M Sodium citrate buffer; pH 7.0-8.0, 0.1 M Potassium phosphate buffer; pH 8.5, 0.1 M Tris-HCl buffer; pH 10.0-11.0, 0.1 M Carbonate-bicarbonate buffer.

    pH activity of GPO.
    The buffer conditions with various pH values were used in the reaction at 37°C. pH 4.0-6.0, 0.1 M Sodium citrate buffer; pH 7.0-8.0, 0.1 M Potassium phosphate buffer; pH 8.5, 0.1 M Tris-HCl buffer; pH 10.0-11.0, 0.1 M Carbonate-bicarbonate buffer.

    Temperature activity of GPO. The enzyme reactions in 0.2 M KH2PO4-NaOH, pH 7.0, were carried out under different temperatures.

    Temperature activity of GPO.
    The enzyme reactions in 0.2 M KH2PO4-NaOH, pH 7.0, were carried out under different temperatures.

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