Luminescence immunoassay

Hamilton Umicon Lumicon chemi- and biolumium assay luminometer This equipment is used in test-tube scale luminescent immunoassays. With its sample compartment (thermostatted by means of Peltier elements, which allow the temperature to be set from 15°C to 40°C with a precision of 0.1°K) this instrument is suitable for the measurement of temperature-sensitive bioluminescence resulting from enzymic reactions and also in phagocyte-mediated luminescence measurements. 

K. Van Dyke and R. Van Dyke, eds., Luminescence Immunoassay and Molecular Applications, CRC Press, Boca Raton, Florida (1990). 

Hardcastle, A., W. Aherne, and V. Marks (1988). A sensitive enhanced luminescent immunoassay for the triazine pesticides atrazine and simazine. J. Biolumin. Chemilumin., 2 209. 

Following this study, Korovin and coworkers tested cryptands 23b-f which are used in time-resolved luminescent immunoassays (Mathis, 1993) for the sensitization of Ybm luminescence (Korovin et al., 2002b). From the lifetimes determined in both water and deuterated water, one calculates that the hydration number varies from 2 (23b), to 1.5 (23a, 23e), and finally to 1 (23c, 23d, 23f). Quantum yields were not determined, but luminescence intensities relative to the cryptate with 23a (in water, at room temperature) point to cryptands 23c and 23d being the best sensitizers of the Yb111 luminescence with a seven-fold enhancement, while cryptates with 23e and 23b are only 1.5- to 1.8-times more luminescent. 

II. Ikariyama, Y., Suzuki, S., andAizawa, M., Luminescence immunoassay of human serum albumin with hemin as labeling catalyst. Anal. Chem. 54, 1126-1129 (1982). 

A recent example of this consideration is the success of [Eu C bpy.bpy.bpy] cryptate in luminescence immunoassay (104). This cryptate is used as a label to an antibody that is coupled in a specific way to a biomolecule, the presence of which has to be proved. TTie structure of the molecule is shown in Fig. 47. Excitation is into the bpy molecule, which shows a very high absorption strength in the ultraviolet part of the spectrum (cmax 10 M cm ). From the bpy triplet state the energy is transferred to the Eu ion, which finally emits (104,107). Although the quantum efficiency is only 1% (104), the high bpy absorption strength makes application feasible. 

Most immunoassays currently employed in the biomedical field are either radioimmunoassays, enzyme immunoassays, or luminescence immunoassays (including fluorescence immunoassays [FIA] and chemiluminescence immunoassays). Although radioimmunoassay is currently the most sensitive of these (10 -10 M concentrations are often detectable), due to the problems inherent to dealing with radioactive materials, such as licensing, radiation hazard, short shelf-life of expensive radioisotopes, the expense of the counting equipment, and the tedium associated with heterogeneous immunoassay, it has fallen, in popularity, behind the non-isotopic methods of analysis. 

Karnes, H.T. O Neal, J.S. Schulman, S.G. Luminescence immunoassay. In Molecular Luminescence Spectroscopy Methods and Applications Part 1 Schulman, S.G., Ed. Wiley-Interscience New York 1985 Chap. 8. 

Zucchelli G, Pilo A, Prontera C, et al. Evaluation of a luminescence immunoassay for the measurement of human thyroglobulin. Clin Chem 1990 36 1083. 

Hughes J, Weston S, Montague D, Summers M, Shepard H, Shepard B. Enhanced luminescence immunoassay for estradiol. Clin Chem 1989 35 ... 

Fukada, H., A. Haga, T. Fujita, N. Hiramatsu, C.V. Sullivan and A. Hara. Development and validation of chemi-luminescent immunoassay for vitellogenin in five salmonid species. Comp. Biochem. Physiol. 130A 163-170, 2001. 

ILA23 A Radioimmunoassays and Enzyme, Fluorescence, and Luminescence Immunoassays... 

Armbruster, D. A., Jirinzu, D. C., and Williams, J. V., Enhanced luminescence immunoassays for free thyroxine (FT4). Clin. Chem. (Winston-Salem, N.C.) 34, 1153-1154 (abstr.) (1988). Amhold, J., Mueller, S., Arnold, K., and Grimm, E., Chemiluminescence intensities and spectra of luminol oxidation by sodium hypochlorite in the presenee of hydrogen peroxide. J. Biolumin. Chemilumin. 6, 189-192 (1991). 

Billing, J., Hinchy, V., and Montague, D., Enhanced luminescence immunoassay for creatine kinase MB (CK-MB). Clin. Chem. (Winston-Salem, N.C.) 36, 1130 (abstr.) (1990). 

Brestel, E. P., Co-oxidation of luminol by hypochlorite and hydrogen peroxide. Implications for neutrophil chemiluminescence. Biochem. Biophys. Res. Commun. 126, 482-488 (1985). Brolin, S., and Wetteimark, G., Bioluminescence Analysis. VCH Verlag, Weinheim, 1992. Bronstein, L, Chemiluminescent 1,2-dioxetane-based enzyme substrates and their applications. In Luminescence Immunoassay and Molecular Applications (K. Van Dyke and R. Van Dyke, eds.), pp. 255-274. CRC Press, Boca Raton, FL, 1990. 

KIO. Kinkel, T., Lubbers, H., Schmidt, E., Molz, P., and Skrzipczyk, H. J., Synthesis and properties of new luminescent acridinium-9-carboxyiic acid derivatives and their applications in luminescence immunoassays (LIA). J. Biolumin. Chemilumin. 4, 135-139 (1989). 

L14. Longeon, A, Henry, J. P., and Henry, R., A solid-phase luminescent immunoassay for human chorionic gonadotrophin using Pholas dactylus bioluminescence. J. Immunol. Methods 89, 103-109 (1986). 

M29. Messeri, G., Orlandini, A., and Pazzagli, M., Luminescent immunoassay using isoluminol derivatives. J. Biolumin. Chemilumin. 4, 154-158 (1989). 

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