QUANTITATION OF ENZYMES AND THEIR SUBSTRATES in Visual Studio .NET

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QUANTITATION OF ENZYMES AND THEIR SUBSTRATES
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potential of 700 mV versus saturated calomel electrode (SCE) to produce molecular oxygen: H 2 O 2 2 H O 2 2 e 3:26
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The electrons produced in this oxidation reaction result in a measured current that is directly proportional to H2O2 concentration. Amperometry has been used to quantitate inorganic phosphate (Pi)17 in a dualenzyme assay, shown in Eqs. 3.27 and 3.28: Phosphate Inosine Ribose-1-phosphate Hypoxanthine ! 3:27 Hypoxanthine 2 H2 O O2 ! Uric acid H2 O2
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xanthine oxidase nucleoside phosphorylase
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In addition to peroxide-producing reactions, amperometry may be used in conjunction with a variety of oxidase and dehydrogenase enzymes that employ low molecular weight mediators (Med) as electron acceptors in place of molecular oxygen. ! Sred n Med ox Pox n Med red
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Ferricinium derivatives, ferricyanide, a variety of quinone derivatives, and other organic oxidants have been used as mediators of oxidase and dehydrogenase reactions. Following their reduction in solution, these mediators are reoxidized at a working electrode, yielding measurable currents. Electron-transfer mediators that posses fast rates of heterogeneous (electrochemical) electron transfer have been shown to yield better S/N than oxygen/hydrogen peroxide mediation. 3.5.2.2. Potentiometry. Potentiometric methods rely on the logarithmic relationship between measured potential and analyte concentration. The most common involves an instrument called a pH-Stat , in which a glass (pH) electrode follows reactions that either consume or produce protons. Since pH changes cause changes in enzyme activity, the pH is maintained at a constant value by the addition of acid or base. The rate of titrant addition is then proportional to the rate of the enzymatic reaction. Precise measurements using the pH-Stat require low buffer concentrations in the enzymatic assay mixture. Other potentiometric methods employ gas-sensing electrodes for NH3 (for deaminase reactions) and CO2 (for decarboxylase reactions). Ion-selective electrodes have also been used to quantitate penicillin, since the penicillinase reaction may be mediated with I or CN . 3.5.2.3. Conductimetry. These methods involve the application of an alternating voltage across two electrodes in solution, and the measurement of the
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magnitude of the alternating current response. This current is directly proportional to the conductivity of the solution, which, in turn, is dictated by ionic strength. The urease reaction, in particular, is ideally suited to conductimetric quantitation.18 Urea is hydrolyzed by urease according to Eq. 3.31: H2 NCONH2 3 H2 O 2 NH HCO OH ! 4 3
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In this reaction, four ions are produced from a single uncharged molecule of substrate, resulting in a signi cant increase in ionic strength. Good S/N may be achieved if the initial ionic strength (buffer concentration) of the assay medium is low, in the 5 10-mM range. 3.5.3. Other Detection Methods 3.5.3.1. Radiochemical. Radiochemical methods are increasingly becoming supplanted by methods that do not require specialized facilities, although in some cases, the method of choice still involves the use and quantitation of radioactive species. Examples include the endpoint assays for guanosine-50 -triphosphate (GTP) and guanosine-50 -diphosphate (GDP).19 These species are involved in hormone regulation, protein synthesis and secretion, and gluconeogenesis. The GTP assay involves Reactions 3.32 and 3.33:
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Aspartate 14 C a-Ketoglutarate Oxaloacetate 14 C Glutamate ! 3:32 Oxaloacetate 14 C GTP ! PEP 14 C GDP CO2
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where Phosphoenolpyruvate PEP. All reagents are added in excess, and the mixture is equilibrated overnight with the GTP sample, so that the quantity of PEP 14 C produced is limited by the quantity of GTP present in the sample and the equilibrium constants of the enzymatic reactions. The labeled PEP is then separated by anion-exchange chromatography and quantitated in a scintillation counter. The assay for GDP is conducted using the same reactions in reverse (both enzymes are reversible, and yield an equilibrium mixture of reactants and products), and labeled PEP as a reagent. This reaction is followed by the separation and quantitation of labeled aspartate. Note that all radiochemical enzymatic assays require a separation step prior to quantitation. 3.5.3.2. Manometry. Simple manometric methods may be used in endpoint assays, to measure the total quantity of a gas (such as NH3 or CO2) produced in an enzymatic reaction. Automated manometers may be used in a kinetic mode, to quantitate gas evolution as a function of time. These methods are based on the ideal gas law, which states that the volume occupied by a gas is directly proportional to the number of moles of the gas at constant pressure and temperature. The gas volume is thus measured as a function of time or following completion
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