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An assay for adenosine involves the primary enzyme adenosine deaminase, and a chemical indicator reaction that consumes ammonia by reaction with the ninhydrin reagent (Eq. 3.4):
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The product of this reaction absorbs visible light, with a maximum at 546 nm. The ninhydrin indicator reaction3 may be employed with virtually any primary reaction that produces NH3. The most commonly used indicator enzymes are dehydrogenases and peroxidases. The reactions catalyzed are shown in Eq. 3.5.
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Reduced substrate NAD P Oxidized substrate NAD P H H ! 3:5 ! Reduced dye H2 O2 Oxidized dye H2 O
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peroxidase dehydrogenase
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Dehydrogenases are used in cases where the primary enzymatic reaction produces the reduced substrate for a particular dehydrogenase enzyme reaction. These species are then converted to their oxidized forms in the indicator reaction, where the
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QUANTITATION OF ENZYMES AND THEIR SUBSTRATES
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Figure 3.1. Absorption spectra of the nicotinamide coenzymes.4 [Reprinted, with permission, from H. Netheler, in Methods of Enzymatic Analysis, Wiley-VCH, 1983, Vol. 1, Edited by Hans Ulrich Bergmeyer, 3rd English Edition, # Verlag Chemie GmbH, Weinheim, 1983.]
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formation of reduced nicotinamide coenzyme (NADH or NADPH) allows absorbance measurements at 340 nm, where the molar absorptivities4 of the reduced coenzymes are 6:2 103 M 1 cm 1 (Fig. 3.1). Dehydrogenase indicator reactions are common because few interferences exist for absorbance measurements at 340 nm. Peroxidase indicator reactions may be used to follow any primary reaction that produces hydrogen peroxide. Peroxidases are very speci c for H2O2, but will react with a variety of organic dye species that are colorless in the reduced form, but highly absorbing in the oxidized form. Examples include 2,4-dichlorophenol, Odianisidine, malachite green, and benzidine. Two commercial enzymatic assays exist for the determination of glucose in serum. One involves the primary enzyme glucose oxidase and the indicator enzyme peroxidase: Glucose O2 d-D-Gluconolactone H2 O2 ! 3:7 3:8 The oxidized form of O-dianisidine is red, and shows an absorbance maximum at 450 nm with a molar absorptivity5 of 8:6 103 M 1 cm 1 . The second glucose assay involves hexokinase as a primary enzyme, and uses glucose-6-phosphate (G6P) dehydrogenase as an indicator enzyme: Glucose ATP G6P ADP ! G6P NADP
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O-Dianisidine H2 O2 2; 20 -Dimethoxydiphenylquinonediimine 2H2 O !
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6-Phosphoglyceric acid NADPH H !
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Based on the molar absorptivities of the products, the glucose oxidase peroxidase assay may be expected to yield higher sensitivity and a lower detection limit. Ideally, the indicator enzyme converts primary product into measured product in a linear manner, meaning that every molecule of primary product is instantaneously converted, regardless of substrate concentration. To accomplish this, primary product concentrations are kept low, so that they fall into the linear region of the saturation kinetics curve. For linear conversion at all analyte (primary substrate) concentrations, the effective rate of the indicator reaction, (Veff)ind, must equal Vmax for the primary reaction: Vmax prim Veff ind Vmax ind =f1 Km;P1 = P1 Km;S2 = S2 g 3:11
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Since Km;P1 is a characteristic of the indicator enzyme, and [P1] is dictated by the analyte concentration, the only variables that can be controlled experimentally are Vmax ind , which is equal to kcat Eind (cf. 2) and the cosubstrate concentration [S2]. For this reason, a large excess (100-fold or more) of indicator enzyme is employed, in addition to saturating levels of cosubstrate (O-dianisidine in Eq. 3.8, and NADP in Eq. 3.10). When making initial rate measurements with coupled enzyme systems, there is often a signi cant lag time during which the linkage products build up to steadystate concentrations.6 Remember that some dehydrogenase reactions possess unfavorable equilibria; lactate dehydrogenase, for example, which catalyzes the reaction shown in Eq. 3.12: Lactate NAD Pyruvate NADH H 3:12
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prefers to convert pyruvate to lactate K 5 10 5 at pH 7. For this reason, coupling lactate dehydrogenase to a lactate-producing enzyme will not be effective, unless a trapping reagent is used to remove pyruvate and force the reaction towards products. For example, at pH 9.5, phenylhydrazine will trap pyruvate to produce a phenylhydrazone, shifting the lactate dehydrogenase equilibrium to K 2 10 2 .7 Alternatively, NADH may be trapped with an electron-transfer reagent such as phenazine methosulfate (PMS), which is colorless in the oxidized form but absorbs at 388 nm in the reduced form. 3.4. CLASSIFICATION OF METHODS Enzymatic assay methods are classi ed as xed-time assays, xed-change assays, or kinetic (initial rate) assays. Kinetic assays continuously monitor concentration as a function of time; pseudo- rst-order conditions generally apply up to $ 10% completion of the reaction to allow the initial reaction rate to be determined. If the initial substrate concentration is >10Km, then the initial rate is directly proportional to enzyme concentration. At low initial substrate concentrations (< 0:1 Km ), the initial rate will be directly proportional to initial substrate concentration (cf. 2). For enzyme quantitation, a plot of initial rate against [E] provides a linear
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