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(c) Three potential interferents are shown below in structures D, E, and F (Eq. 6.21). Which of these is likely to present the greatest cross-reactivity in the competitive sandwich immunoassay, and which is expected to present the least cross-reactivity Why
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(d) Draw a plot of label signal versus log[testosterone] that would be expected in this type of assay. 5. Biotin de ciency results from a number of inborn errors of metabolism, and biotin quantitation therefore represents a general screening method for these diseases. Recently, a new method was proposed for biotin quantitation in serum. The method has been called an ELLSA, and relies on the following competitive reaction: Biotins Biotinf Avidin-E Biotins : Avidin-E Biotinf : Avidin-E ! where Biotins and Biotinf are the adsorbed and free (analyte) forms of biotin, respectively, Avidin-E is an Avidin alkaline phosphatase conjugate that is added in limited quantity. Following an incubation period, reagents not bound to the microtiter plates are rinsed away, and the remaining enzyme activity is quantitated using a xed time method after the addition of excess substrate. (a) Sketch the plot of enzyme activity versus log[Biotinf] that would be expected for this type of assay. (b) A synthetic substrate (I, below) was used for enzyme activity measurements. This substrate undergoes dephosphorylation in the presence of alkaline phosphatase to yield an unstable intermediate (II) that decomposes in a chemiluminescent reaction (Eq. 6.22):
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If the Km of alkaline phosphatase for compound I is 0.10 mM, what concentration of this substrate should be used for the enzyme activity determination (c) Show the plot of light intensity versus time that would be obtained by the continuous measurement of light emitted in a control well, where no free biotin had been added to the reaction mixture. How does this differ from a typical absorbance versus time plot that would be obtained if the substrate yielded a colored (absorbing) product 6. In a heterogeneous sandwich immunoassay employing uorescence excitation transfer (Eq. 6.7 and Fig. 6.6), draw the plots of emission intensity versus log[Ag] that would be expected if emission from (a) F1 and (b) F2 were measured.
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7.1. INTRODUCTION The real-time and in situ quantitation of biologically and environmentally important analytes has long been a goal of analytical research. The need for continuous monitoring of substrates in fermentation broths, pesticides, and environmental contaminants in natural waters, and biochemicals or pharmaceutical metabolites in living organisms has led to extensive activity in the eld of biosensor research. Biosensors are devices, ideally small and portable, that allow the selective quantitation of chemical and biochemical analytes. They consist of two components: the transducer and the chemical recognition element. Chemical recognition is accomplished by exploiting the natural selectivities of biochemical species such as enzymes, antibodies, chemoreceptors, and nucleic acids. In the presence of the analyte, these agents, immobilized at the surface of the transducer, cause a change in a measurable property in the local environment near the transducer surface. The transducer monitors this property, and converts the chemical recognition event into a measurable electronic signal. Transducers may measure electrochemical, optical, thermal, or adsorption processes that change in the presence of the analyte. The rst biosensor was introduced by Clarke in 1962,1 and consisted of an enzyme, glucose oxidase (GO) trapped at the surface of a platinum electrode by a semipermeable dialysis membrane that allowed substrates and products to freely diffuse to and from the enzyme layer, as shown in Figure 7.1. The rate of the enzymatic reaction is proportional to the substrate concentration in the external solution. The conversion of glucose and molecular oxygen to gluconolactone and hydrogen peroxide may be monitored electrochemically, by reoxidizing hydrogen peroxide to molecular oxygen at the surface of the platinum electrode. The generated current depends on the local H2O2 concentration, and therefore on the bulk glucose concentration. The magnitude of the response current of the amperometric glucose biosensor shown in Figure 7.1 depends on four main factors. First, mass-transport kinetics determine the rates at which substrates can be supplied to, and products removed from, the reaction layer in which enzyme is trapped. Second, enzyme kinetics
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Bianalytical Chemistry, by Susan R. Mikkelsen and Eduardo Corton ISBN 0-471-54447-7 Copyright # 2004 John Wiley & Sons, Inc.
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