Enzyme Modulator as Label in Separation-Free Immunoassays: Enzyme Modulator Mediated Immunoassay (EMMIA)

  • T. T. Ngo


Enzyme modulator mediated immunoassay (EMMIA) is a separation-free enzyme amplified immunoassay. The assay uses an enzyme modulator (M) as the tag to label a ligand analyte (L). Such stable covalent enzyme modulator-ligand conjugates (M-L) is capable of modulating the activity of an indicator enzyme by either causing a significant inhibition of the enzyme activity or a dramatic activation.


Dihydrofolate Reductase Pyruvate Carboxylase Enzyme Modulator Transition State Analog Isobutyl Chloroformate 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Abeles, R.H., 1978, Suicide enzyme inactivators, in: “Enzyme-Activiated Irreversible Inhibitors,” N. Seiler, M.J. Jung and J. Koch-Weser, eds., pp. 1–12., Elsevier North Holland Biomedical Press, Amsterdam.Google Scholar
  2. Arnon, R., 1977, Immunochemistry of Iysozyme, in: “Immunochemistry of Enzymes and Their Antibodies,” M.R.J. Galton, editor, pp. 1–28, Wiley, New York.Google Scholar
  3. Bacquet, C and Twumasi, D.Y., 1984, A homogeneous enzyme immunoassay with avidin-ligand conjugate as the enzyme-modulator. Anal. Biochem., 136:487–490.PubMedCrossRefGoogle Scholar
  4. Baker, B.R., 1967, “Design of Active-Site-Directed Irreversible Enzyme Inhibitors,” Wiley, New York.Google Scholar
  5. Blecka, L.J., Shaffar, M., 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, eds., 207–214, Elsevier Science Publishers, Amsterdam.Google Scholar
  6. Cinader, B., 1976, Enzyme-antibody interactions, in: Methods of Immunology and Immunochemistry, Chase M. & Williams C., editors, pp. 313–375. Academic Press, New York.Google Scholar
  7. Finley, P.R., Williams, R.J. and Lichti, D.A., 1980, Evaluation of a new homogeneous enzyme inhibitor immunoassay of serum throxine with use of a bichromatic analyzer. Clin. Chem. 26:1723–1726.PubMedGoogle Scholar
  8. Gonnelli, M., Gabellieri, E., Montagnoli, G. and Felicioli, R., 1981, Complementing S-peptide as modulator in enzyme immunoassay. Biochem. Biophys. Res. Commun. 103:917–923.CrossRefGoogle Scholar
  9. Green, N.M., 1975, Avidin, in: Advances in Protein Chemistry, C.B. Anfisen, J.T. Edsall and F.M. Richards, editors, pp. 85–133, Academic Press, New York.Google Scholar
  10. Iwert, M.E., Nelson, N.S and Rust, J.H., 1967, Some immunologic properties of Jackbean urease and its antibody. Archs. Biochem. Biophys. 122:95–104.CrossRefGoogle Scholar
  11. Kennett, R.H., McKearn, J.J. and Bechtol, K.B., editors, 1980, Monoclonal Antibodies, Hybridoma: A New Dimension in Biological Analyses, Plenum Press, New York.Google Scholar
  12. Kohler, G. and Milstein, C., 1975, Continuous cultures of fused cells secreting antibody of predefined specificity, Nature, 156:495–497.CrossRefGoogle Scholar
  13. Krebs, E.G., 1972, Protein kinases, in: Current Topics in Cellular Regulation, B.L. Horecker and E.R. Stadtman, editors, pp. 99–133, Academic Press, New York.Google Scholar
  14. Ngo, T.T. (1983) Enzyme modulator mediated immunoassay (EMMIA), Int. J. Biochem., 15:583–590.PubMedCrossRefGoogle Scholar
  15. Ngo, T.T. and Lenhoff, H.M., 1980, Enzyme modulators as tools for the development of homogeneous enzyme immunoassays, FEBS Lett., 116:285–288.PubMedCrossRefGoogle Scholar
  16. Ngo, T.T. and Lenhoff, H.M., 1982, Enzymes as versatile labels and signal amplifiers for monitoring immunochemical reactions, Molec. Cell Biochem. 44:3–12.PubMedCrossRefGoogle Scholar
  17. Ngo, T.T. and Tunnicliff, G., 1981, Inhibition of enzymic reactions by transation state analogs: An approach for drug design, Gen. Pharmac. 12:129–138.CrossRefGoogle Scholar
  18. 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. Method, 61:209–216.CrossRefGoogle Scholar
  19. Richards, F.M. and Vithayathil, P.J., 1959, The preparation of subtilisin-modified ribonuclease and the separation of the peptide and protein components, J. Biol. Chem., 234:1459–1465.PubMedGoogle Scholar
  20. 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., 27:1979–1806.Google Scholar
  21. Shaw, E.N., 1980, Design of irreversible inhibitors, in: Enzyme Inhibitor as Drugs, M. Sandler, editor, pp. 24–42, University Park Press, Baltimore.Google Scholar
  22. Stadtman, E.R., 1970, Mechanisms of enzyme regulation in metabolism, in: The Enzymes, P.D. Boyer, editor, Vol. 1, pp. 397–459, Academic Press, New York.Google Scholar
  23. Webb, J.L., 1963, Enzyme and metabolic inhibitors, Vols 1–3, Academic Press, New York.Google Scholar
  24. Wolfenden, R., 1969, Transition state analogs for enzyme catalysis, Nature, 223:704–705.PubMedCrossRefGoogle Scholar
  25. Wolfenden, R., 1972, Analog approaches to the structure of the transition state in enzyme reactions. Acc. Chem. Res., 5:10–18.CrossRefGoogle Scholar
  26. Wong, J.T.F., 1975, Kinetics of Enzyme Mechanisms, pp. 39–72, Academic Press, New York.Google Scholar

Copyright information

© Plenum Press, New York 1985

Authors and Affiliations

  • T. T. Ngo
    • 1
  1. 1.Department of Developmental and Cell BiologyUniversity of CaliforniaIrvineUSA

Personalised recommendations