Abstract
Out of a variety of enzymes which have been described according to their kinetics and structure only a few have turned out to be marker enzymes in the enzyme immunoassay (EIA). The ones that are mostly used are horseradish peroxidase (HRP), calf intestinal alkaline phosphatase (AP) and ß-galactosidase from E. coli (ßGal). The suitability of enzymes as markers is not only determined by their great molar activity that is to be largely maintained even after binding to immunoreactants, their stability and commercial availability but especially by their simple, practicable and sensitive detectability.
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References
Al-Kaissi, E. and Mostratos, A., 1983, Assessment of substrates for horseradish peroxidase in enzyme immunoassay, J. Immunol. Methods, 58: 127–132.
Ames, B.N., Kämmen, H.O., and Yamasaki, E., 1975, Hairdyes are mutagenic: Identification of a variety of mutagenic ingredients, Proc. Natl. Acad. Sci., 72: 2423–2427.
Artiss, J.D., McGowan, M.W., Strandbergh, D.R., and Zak, B., 1982, A procedure for the kinetic colorimetric determination of serum cholinesterase activity, Clin. Chim. Acta, 124: 141–148.
Artiss, J.D., Strandbergh, D.R., and Zak, B., 1983, On the use of a sensitive indicator reaction for the automated glucose oxidase-peroxidase coupled reaction, Clin. Biochem., 16: 334–337.
Barham, D., and Trinder, P., 1972, An improved color reagent for the determination of blood glucose by the oxidase system, Analyst, 97: 142–145.
Bos, E.S., van der Doelen, A.A., van Rooy, N., and Schuurs, A.H.W.M., 1981, 3,3, 5,5-tetramethylbenzidine as an Ames test negative chromogen for horse-radish peroxidase in enzyme-immunoassay, J. of Immunoassay, 2: 187–204.
Capaldi, D.J., and Taylor, K.E., 1983, A new peroxidase color reaction: Oxidative coupling of 3-methyl-2-benzothiazoline hydrazone (MBTH) with its formaldehyde azine. Application to glucose and choline oxidases, Anal. Biochem., 129: 329–336.
Chandler, H.M., Cox, J.C., Healey, 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. Methods, 53: 187–194.
Chandler, H.M., and Hurell, G.R., 1982, A new enzyme immunoassay system suitable for field use and its application in a snake venom detection kit, Clin. Chim. Acta, 121: 225–230.
Cox, C., 1983, NAD labeled immunoassays, Trends in Anal. Chem., 2: 129–131.
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. Methods, 82: 65–75.
Ellens, D.J., and Gielkens, A.L.J., 1980, A simple method for the purification of 5-aminosalicylic acid. Application of the product as substrate in enzyme-linked immunosorbent assay (ELISA), J. Immunol. Methods, 37: 325–332.
Gallati, H., 1977, Aktivitätsbestimmung von Peroxidase mit Hilfe des “Trinder-Reagens”, J., Clin. Chem. Clin. Biochem., 15: 699–703.
Gallati, H., 1979, Peroxidase aus Meerrettich: Kinetische Studien sowie Optimierung der Aktivitätsbestimmung mit den Substraten H2O2 und ABTS, J. Clin. Chem. Clin. Biochem., 17: 1–7.
Gallati, H., and Brodbeck, H., 1982a, Peroxidase aus Meerrettich: Kinetische Studien und Optimierung der Aktivitätsbestimmung mit den Substraten H2O2 und o-Phenylendiamin, J.Clin. Chem. Clin. Biochem., 20: 221–225.
Gallati, H., and Brodbeck, H., 1982b, Peroxidase aus Meerrettich: Reagens zum Abstoppen der katalytischen Umsetzung der Substrate H2O2 und 2,2′-Azino-di(3-ethyl-benzthiazolinsulfonsäure-(6) (ABTS), J. Clin. Chem. Clin. Biochem., 20: 757–760.
Gallati, H., and Pracht, J., 1985, Peroxidase aus Meerrettich: Kinetische Studien und Optimierung der Peroxidase-Aktivitätsbestimmung mit den Substraten H2O2 und 3,3′, 5,5′-Tetramethylbenzidin, J. Clin. Chem. Clin. Biochem., 23: 435–460.
Geoghegan, W.D., Struve, M.F., and Jordon, R.E., 1983, Adaption of the Ngo-Lenhoff Peroxidase assay for solid phase ELISA, J. Immunol, Methods, 60: 61–68
Gochman, N., and Schmitz, J.M., 1971, Automated determination of uric acid with use of a uricase-peroxidase system, Clin. Chem., 17: 1154–1159.
Harper, J.R., and Orengo, A., 1981, The preparation of an immuno-globulin-amyloglucosidase conjugate and its quantitation by an enzyme-cycling assay, Anal. Biochem., 113: 51–57.
Hofmann, F., Hubl, W., and Schütting, R., 1983, Eine mechanisierte Bestimmungsmethode für Meerrettich-Peroxidase am Reaktionsgeschwindigkeitsanalysator mit den Chromogenen o-Dianisidin und o-Phenylendiamin zur Anwendung beim ELISA, Z. med. Labor,-Diagn., 24: 155–160.
Hofmann, J., and Sernetz, M., 1984, Immobilized enzyme kinetics analyzed by flow-through microfluorimetry. Resorufin-ß-D-galactopyranoside as a new fluorogenic substrate for ß-galactosidase, Anal. Chim. Acta, 163: 67–72.
Hildebrandt, A., 1986, Verfahren zur Bestimmung der Enzymaktivität gelöster und trägergebundener Peroxidase-markierter Antikörper, Z. med. Labor.-Diagn., 6: 149–153.
Johannsson, A., Stanley, Ch. J., and Seif, H.C., 1985, A fast highly sensitive colorimetric enzyme immunoassay system demonstrating benefits of enzyme amplification in clinical chemistry, Clin. Chim. Acta., 148: 119–124.
Klapper, M.H., and Hackett, D.P., 1963, The oxidatic activity of horseradish peroxidase. I. Oxidation of hydro-and naphthohydroquinones, J. Biol. Chem., 238: 3736–3742.
Lin, E.H., and Gibson, D.M., 1977, Visualization of peroxidase isoenzymes with eugenol, a noncarcinogenic substrate, Anal. Biochem., 79: 597–601.
McGowan, M.W., Artiss, J.D., Strandbergh, D.R., and Zak, B., 1983, A peroxidase-coupled method for the colorimetric determination of serum triglycerides, Clin. Chem., 29: 538–542.
Meiattini, F., Prenzipe, L., Bardelli, F., Giannini, G., and Tarli, P., 1978, The 4-hydroxybenzoate/4-aminophenazone chromogenic system used in the enzymic determination of serum cholesterol, Clin. Chem., 24: 2161–2165.
Moss, D.W., Self, C.H., Whitaker, K.B., Bailyes, E., Siddle, K., Johannson, A., Stanley, C.J., and Cooper, E.H., 1985, An enzyme-amplified monoclonal immuno-enzymometric assay for prostatic acid phosphatase, Clin. Chim. Acta., 152: 85–94.
Ngo, T.T., and Lenhoff, H.M., 1980, A sensitive and versatile chromogenic assay for peroxidase and peroxidase-coupled reactions, Anal. Biochem., 105: 389–397.
Orsonneau, J.L., Meflah, K., Lustenberger, P., Cornu, G., and Bernard, S., 1982, Sensitation and visualisation of biochemical measurements using the NAD/NADH system by means of Meldola blue. I. Principle and application to the continous flow measurement of LDH and HBDH activities in serum, Clin. Chim. Acta, 125: 177–184.
Paul, K.G., Ohlsson, P.J., and Jönsson, N.A., 1982, The assay of peroxidases by means of dicarboxidine on enzyme-linked immunosorbent assay level, Anal. Biochem., 124: 102–107.
Persijn, J.P., and Jonker, K.M., 1978, A terminating reagent for the peroxidase-labelled enzyme immunoassay, J. Clin. Chem. Clin. Biochem., 16: 531–532.
Porstmann, B., Porstmann, T., and Gaede, D., 1980, Optimierung der Aktivitätsbestimmung von Meerrettichperoxidase, Z. med. Labor.-Diagn., 21: 201–209.
Porstmann, B., Porstmann, T., Gaede, D., Nugel, E., and Egger, E., 1981a, Temperature dependent rise in activity of horseradish peroxidase caused by non-ionic detergents and its use in enzyme-immunoassay, Clin. Chim. Acta, 109: 175–181.
Porstmann, B., Porstmann, T., and Nugel, E., 1981b, Comparison of chromogens for the determination of horseradish peroxidase as a marker in enzyme immunoassay, J. Clin. Chem. Clin. Biochem., 19: 435–439.
Porstmann, B., Porstmann, T., Nugel, E., and Evers, U., 1985a, Which of the commonly used marker enzymes gives the best results in colorimetric and fluorimetric enzyme immunoassays: horseradish peroxidase, alkaline phosphatase or ß-galactosidase, J. Immunol. Methods 79: 27–37.
Porstmann, T., Porstmann, B., Wietschke, R., von Baehr, R., and Egger, E., 1985b, Stabilization of the substrate reaction of horseradish peroxidase with o-phenylenediamine in the enzyme immunoassay, J. Clin. Chem. Clin. Biochem., 23: 41–44.
Pradelles, Ph., Grassi, J., and Maclouf, J., 1985, Enzyme immunoassay of eicosanoids using acetylcholine esterase as label: an alternative to radioimmunoassay, Anal. Chem., 57: 1170–1173.
Rathlev, T., and Franks, G.F., 1982, New procedure for detecting antinuclear antibodies using glucose oxidase immunoenzyme technique, Am. J. Clin. Pathol., 677: 705–709.
Stanley, C.J., Paris, F., Plumb, A., Webb, A., and Johannson, A., 1985, Enzyme amplification: A new technique for enhancing the speed and sensitivity of enzyme immunoassays, Int. Clin. Prod. Rev., 7/8: 44–51.
Teshima, Sh., Mitsuhida, N., and Ando, M., 1985, Determination of-amylase in biological fluids using a new substrate (ß-2-chloro-4-nitrophenyl-maltopentaoside), Clin. Chim. Acta, 150: 165–174.
Trinder, P., 1969, Determination of glucose in blood using glucose oxidase with an alternative oxygen acceptor, Ann. Clin. Biochem., 6: 24–27.
Werner, W., Rey, H.-G., and Wielinger, H., 1970, Über die Eigenschaften eines neuen Chromogens für die Blutzuckerbestimmung nach der GOD/POD-Methode, Z. Anal. Chemie, 252: 224–228.
Wimmer, M.C., Artiss, J.D., and Zak, B., 1985, Peroxidase coupled method for kinetic colorimetry of total creatine kinase activity in serum, Clin. Chem., 31: 1616–1620.
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© 1988 Plenum Press, New York
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Porstmann, B., Porstmann, T. (1988). Chromogenic Substrates for Enzyme Immunoassay. In: Ngo, T.T. (eds) Nonisotopic Immunoassay. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5466-6_3
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DOI: https://doi.org/10.1007/978-1-4684-5466-6_3
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