Abstract
Separation-free enzyme immunoassays for both haptens and macromolecules have been developed by using enzyme modulator as the label (Ngo and Lenhoff, 1980; Ngo, 1983; Finley et al., 1980; Place et al., 1983; Blecka et al., 1983; Bacquet and Twumasi, 1984; Brontman and Meyerhoff, 1984; Dona, 1985). In this chapter, enzyme modulators are defined as compounds capable of bringing about the modifications of the catalytic activity of an enzyme by inhibiting or enhancing (activating) the enzyme activity. The modification of an enzyme activity by enzyme modulators can be achieved through either noncovalent or covalent interactions between the enzyme and its modulators. Non-covalently interacting modulators are generally reversible modulators, such as reversible low molecular weight enzyme inhibitors (Webb, 1963) or enzyme activators (Wong, 1975), allosteric effectors (Stadtman, 1970), transition state analogs (Wolfenden, 1972; Lienhard, 1973; Ngo and Tunnicliff, 1981) and inhibitory antibodies to an enzyme (Marucci and Mayer, 1955; Visek et al., 1967; Cinader, 1976; Arnon, 1977). Covalently interacting enzyme modulators consist of irreversible modulators such as activesite directed irreversible enzyme inhibitors (Baker, 1967; Shaw, 1980), mechanism based inhibitors (Rando, 1974; Abeles, 1978) and enzyme mediated modification of enzyme activity (Krebs, 1972).
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Abeles, R. H., 1978, Suicide enzyme inactivators, in: “Enzyme-Activated Irreversible Inhibitors”, N. Seiler, M.J. Jung and J. Koch-Weser, editors, pp. 1–12, Elsevier/North-Holland Biomedical Press, Amsterdam.
Alexander, P.W. and Maltra, C., 1982, Enzyme-linked immunoassay of human immunoglobulin G with the fluoride ion selective electrode, Anal. Chem. 54;68–71.
Arnon, R., 1977, Immunochemistry of lysozyme, in.: “Immunochemistry of Enzyme and Their Antibodies”, M.R.J. Galton, editor, pp. 1–28, Wiley, New York.
Bacquet, C. and Twumasi, D.Y., 1984, A homogeneous enzyme immunoassay with avidin-ligand conjugate as the enzyme-modulator. Anal. Biochem., 136: 387–490.
Baker, B.R., 1967, “Design of Active-Site Directed Irreversible Enzyme Inhibitors”, Wiley, New York.
Blecka, L.J., Shaffar, M. and Dworschack, R., 1983, Inhibitor Enzyme Immunoassays for quantitation of various haptens: A review, in: “Immunoenzymatic Techniques”, S. Avrameas, P. Druet, R. Masseyeff and G. Feldman, editors, pp. 207–214, Elsevier Science Publishers, Amsterdam.
Boitieux, J.L., Desmet, G. and Thomas, D., 1978, Potentiometric determination of hepatitis B surface antigen in biological fluids, Clin. Chim. Acta, 88: 329–336.
Boitieux, J.L., Desmet, G. and Thomas, D., 1979, An antibody electrode, preliminary report on a new approach in enzyme immunoassay, 25: 318–321.
Brontman, S.B. and Meyerhoff, M.E. 1984, Homogeneous enzyme-linked assays mediated by enzyme antibody; a new approach to electrode-based immunoassays, Anal. Chim. Acta, 162: 363–367.
Broyles, C.A. and Rechnitz, G.A., 1986, Drug antibody measurement by homogeneous enzyme immunoassay with amperometric detection, Anal. Chem., 58: 1242–1245.
Caras, S. and Janata, J., 1980, Field effect transitor sensitive to penicillin, Anal. Chem., 52: 1935–1937.
Chandler, H.M., Cox, J.C., Healy, K., MacGregor, A., Premier, R.R. and Hurrell, J.G.R., 1982, An investigation of the use of urease-antibody conjugates in enzyme immunoassays, J. Immunol. Meth., 53: 187–194.
Cheng, F.S. and Christian, G.D., 1977, Amperometric measurement of enzyme reactions with an oxygen electrode using oxidation of reduced nicotinamide adenine dinucleotide, Anal. Chem., 49: 1785–1788.
Cheng, F.S. and Christian, G.D., 1979, A coupled enzymatic method to measure blood lactate by amperometric monitoring of the rate of oxygen depletion with a Clark oxygen electrode, Anal. Chim. Acta, 91: 295–301.
Cinader, B., 1976, Enzyme-antibody interaction, In: “Methods of Immunology and immunochemistry”, M. Chase and C. Williams, editor, pp. 313–375, Academic Press, New York.
Dona, V., 1985, Homogeneous colorimetric enzyme inhibition immunoassay for Cortisol in human serum with Fab anti-glucose 6-phosphate dehydrogenase as a label modulator, J. Immunol. Meth., 82: 65–75.
Finley, P.R., Williams, R.J. and Lichti, D.A., 1980, Evaluation of a new homogeneous enzyme inhibitor immunoassay of thyroxine with use of a bichromatic analyzer, Clin. Chem., 26: 1723–1726.
Gebauer, C.R., Meyerhoff, M.E. and Rechnitz, G.A., 1979, Enzyme electrode-based kinetic assays of enzyme activities, Anal. Biochem., 95: 479–482.
Gebauer, C.R. and Rechnitz, G.A., 1982, Deaminating enzyme labels for Potentiometric enzyme immunoassay, Anal. Biochem., 124: 338–348.
Ishikawa, E., Imagawa, M., Hashida, S., Yoshitake, S., Hamaguchi, Y. and Ueno, T., 1983, Enzyme-labeling of antibodies and their fragments for enzyme immunoassay and immunohistochemical staining, J. Imminoassay, 4: 209–327.
Joseph, J.P., 1985, An enzyme microsensor for urea on an ammonia gas electrode, Anal. Chim. Acta, 169: 149–156.
Kennett, R.H., McKearn, J.J. and Bechtol, K.B. editors, 1980, “Monoclonal Antibodies, Hybridoma: A New Dimension in Biological Analysis”, Plenum, Press, New York.
Kennedy, J.H. Kricka, L.J. and Wilding, P., 1976, Proteinprotein coupling reactions and the applications of protein conjugates, Clin. Chim. Acta, 70: 1–31.
Kirstein, D., Kirstein, L. and Scheller, F. 1985, Enayme electrode for urea with amperometric indication: Part 1 — Basic principle, Biosensors, 1: 117–130.
Krebs, E.G., 1972, Protein Kinases, in: “Curent Topics in Cellular Regulation”, B.L. Horecker and E.R. Stadtman, editors, pp. 99–133, Academic Press, New York.
Lienhard, G.E., 1973, Enzymatic catalysis and transition state theory, Science, 180: 149–154.
Lowe, C.R., 1985, An introduction to the concept and technology of Biosensors, Biosensors, 1: 3–16.
Marucci, A.A. and Mayer, M.M., 1955, Quatitative studies on the inhibition of crystalline urease by rabbit antiurease Arch. Biochem. Biophys., 54: 330–340.
Meyerhoff, M.E. and Rechnitz, G.A., 1979, Electrode based enzyme immunoassay using urease conjugates, Anal. Biochem., 95: 483–493.
Ngo, T.T., 1983, Enzyme modulator mediated immunoassay (EMMIA), Int. J. Biochem., 15: 583–590.
Ngo, T.T., 1985, Enzyme modulator as label in separation-free immunoassays: Enzyme modulator mediated immunoassay (EMMIA), in: “Enzyme-Mediated Immunoassay”, T.T. Ngo and H.M. Lenhoff, editors, pp. 52–72, Plenum Press, New York.
Ngo, T.T. and Lenhoff, H.M., 1980, Enzyme modulators as tools for the development of homogeneous enzyme immunoassays, FEBS Letters, 116: 285–288.
Ngo, T.T. and Tunnicliff, G., 1981, Inhibition of enzymic reactions by transition state analogs: An approach for drug design, Gen. Pharmacol, 12: 129–138.
Nikolelis, D.P., Painton, C-D. D. and Mottola, H.A., 1979, The peroxidase-catalysed oxidation of NADH as an indicator reaction for repetitive determinations by by sample injection in closed flow-through systems: The determination of LDH in blood serum, Anal. Biochem., 97: 255–263.
Place, M.A., Carrico, R.J., Yeager, F.M., Albarella, J.P. and Boguslaski, R.C., 1983, A colorimetric immunoassay based on enzyme inhibitor method, J. Immunol. Meth., 61: 209–216.
Rando. R.R., 1974, Chemistry and enzymology of k cat inhibitors, Science, 185: 320–324.
Sevier, D.E., David, G.S., Martinis, J., Desmond, W.J., Bartholomew, R.M. and Wang, R., 1981, Monoclonal antibodies in clinical immunology, Clin. Chem., 22: 1806–1979.
Shaw, E.N., 1980, Design of irreversible inhibitors, in: “Enzyme Inhibitors as Drugs”, M. Sandler, editor, pp. 24–42, University Park Press, Baltimore.
Siddle, K., 1985, Properties and applications of monoclonal antibodies, in: “Alternative Immunoassays”, W.P. Collins, editor, pp. 13–37, Wiley, New York.
Stadtman, E.R., 1970, Mechanism of enzyme regulation in metabolim, in: “The Enzyme”, P.D. Boyer, editor, Vol. 1, pp. 397–459, Academic Press, New York.
Visek, W.J., Iwert, M.E., Nelson, N.S. and Rust, J.H., 1967, Some immunological properties of jack bean urease and its antibody, Arch. Biochem. Biophys., 122: 95–104.
Vora, J.L., 1985, Monoclonal antibodies in enzyme research: Present and potential applications, Anal. Biochem., 144: 307–318.
Webb, J.L., 1963, Enzyme and Metabolic Inhibitors, Vols. 1-3, Academic Press, New York.
Wolfenden, R., 1972, Analog approaches to the structure of the transition state in enzyme reactions, Acc. Chem. Res., 5: 10–18.
Wong, J.T.F., 1975, “Kinetics of Enzyme Mechanism”, pp. 39–72, Academic Press, New York.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1987 Springer Science+Business Media New York
About this chapter
Cite this chapter
Ngo, T.T. (1987). Antibody to an Enzyme as the Modulator in Separation-Free Enzyme Immunoassays with Electrochemical Sensor. In: Ngo, T.T. (eds) Electrochemical Sensors in Immunological Analysis. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1974-8_10
Download citation
DOI: https://doi.org/10.1007/978-1-4899-1974-8_10
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4899-1976-2
Online ISBN: 978-1-4899-1974-8
eBook Packages: Springer Book Archive