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Original Articles

Comparison of Luminescent Immunoassays Using Biotinylated Proteins of Aequorin, Alkaline Phosphatase and Horseradish Peroxidase as Reporters

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Pages 3310-3313 | Received 31 Jul 2008, Accepted 20 Aug 2008, Published online: 22 May 2014

  • 1) Shimomura, O., “Bioluminescence: Chemical Principle and Methods,” World Scientific Publishing, Singapore, pp. 90–133 (2006).
  • 2) Blinks, J. R., Wier, W. G., Hess, P., and Prendergast, F. G., Measurement of Ca2+ concentrations in living cells. Prog. Biophys. Mol. Biol., 40, 1–114 (1982).
  • 3) Inouye, S., Noguchi, M., Sakaki, Y., Takagi, Y., Miyata, T., Iwanaga, S., Miyata, T., and Tsuji, F. I., Cloning and sequence analysis of cDNA for the luminescent protein aequorin. Proc. Natl. Acad. Sci. USA, 82, 3154–3158 (1985).
  • 4) Inouye, S., Sakaki, Y., Goto, T., and Tsuji, F. I., Expression of apoaequorin complementary DNA in Escherichia coli. Biochemistry, 25, 8425–8429 (1986).
  • 5) Inouye, S., Aoyama, S., Miyata, T., Tsuji, F. I., and Sakaki, Y., Overexpression and purification of the recombinant Ca2+-binding protein, apoaequorin. J. Biochem., 105, 474–477 (1989).
  • 6) Shimomura, O., and Inouye, S., The in situ regeneration and extraction of recombinant aequorin from Escherichia coli cells and the purification of extracted aequorin. Protein Expr. Purif., 16, 91–95 (1999).
  • 7) Head, J. F., Inouye, S., Teranishi, K., and Shimomura, O., The crystal structure of the photoprotein aequorin at 2.3 Å resolution. Nature, 405, 372–376 (2000).
  • 8) Toma, S., Chong, K. T., Nakagawa, A., Teranishi, K., Inouye, S., and Shimomura, O., The crystal structures of semi-synthetic aequorins. Protein Sci., 14, 409–416 (2005).
  • 9) Ohashi, W., Inouye, S., Yamazaki, T., and Hirota, H., NMR analysis of the Mg2+-binding properties of aequorin, a Ca2+-binding photoprotein. J. Biochem., 138, 613–620 (2005).
  • 10) Zenno, S., and Inouye, S., Bioluminescent immunoassay using a fusion protein of protein A and the photoprotein aequorin. Biochem. Biophys. Res. Commun., 171, 169–174 (1990).
  • 11) Erikaku, T., Zenno, S., and Inouye, S., Bioluminescent immunoassay using a monomeric Fab′-photoprotein aequorin conjugate. Biochem. Biophys. Res. Commun., 174, 1331–1336 (1991).
  • 12) Zatta, P. F., Nyame, K., Cormier, M. J., Mattox, S. A., Prieto, P. A., Smith, D. F., and Cummings, R. D., A solid-phase assay for β-1,4-galactosyltransferase activity in human serum using recombinant aequorin. Anal. Biochem., 194, 185–191 (1991).
  • 13) Stults, N. L., Stocks, N. F., Rivera, H., Gray, J., McCann, R. O., O’Kane, D., Cummings, R. D., Cormier, M. J., and Smith, D. F., Use of recombinant biotinylated aequorin in microtiter and membrane-based assays: purification of recombinant apoaequorin from Escherichia coli. Biochemistry, 31, 1433–1442 (1992).
  • 14) Sgoutas, D. S., Tuten, T. E., Verras, A. A., Love, A., and Barton, E. G., AquaLite bioluminescence assay of thyrotropin in serum evaluated. Clin. Chem., 41, 1637–1643 (1995).
  • 15) Lewis, J. C., Cullen, L. C., and Daunert, S., Site-specifically labeled photoprotein-thyroxine conjugates using aequorin mutant containing unique cysteine residues: application for binding assay (part II). Bioconj. Chem., 11, 140–145 (2000).
  • 16) Shrestha, S., Paeng, R. I., Deo, K. S., and Daunert, S., Cysteine-free mutant of aequorin as a photolabel in luminoassay development. Bioconj. Chem., 13, 269–275 (2002).
  • 17) Deo, S. K., Lewis, J. C., and Daunert, S., Bioluminescence detection of proteolytic bond cleavage by using recombinant aequorin. Anal. Biochem., 281, 87–94 (2000).
  • 18) Verhaegen, M., and Christophoulous, T. K., Quantitative polymerase chain reaction based on a dual-analyte chemiluminescence hybridization assay for target DNA and internal standard. Anal. Chem., 70, 4120–4125 (1998).
  • 19) Laios, E., Ioannou, P. C., and Christophoulous, T. K., Enzyme-amplified aequorin-based bioluminometric hybridization assays. Anal. Chem., 73, 689–692 (2001).
  • 20) Inouye, S., and Sato, J., Recombinant aequorin with a reactive cysteine residue for conjugation with maleimide-activated antibody. Anal. Biochem., 378, 105–107 (2008).
  • 21) Ito, K., Nishimura, W., Maeda, M., Gomi, K., Inouye, S., and Arakawa, H., Highly sensitive and rapid tandem bioluminescent immunoassay using aequorin-labeled Fab fragment and biotinylated firefly luciferase. Anal. Chim. Acta, 588, 245–251 (2007).
  • 22) Adamczyk, M. A., Moore, J. A., and Shreder, K., Quenching of biotinylated aequorin bioluminescence by dye-labeled avidin conjugates: application to homogeneous bioluminescence resonance energy transfer assays. Bioconj. Chem., 11, 1797–1800 (2001).
  • 23) Inouye, S., and Nakamura, M., Identification of biotinylated lysine residues in the photoprotein aequorin by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry peptide mapping after lysine specific endopeptidase digestion. Anal. Biochem., 316, 216–222 (2003).
  • 24) Verhaegen, M., and Christophoulous, T. K., Bacterial expression of in vivo-biotinylated aequorin for direct application to bioluminometric hybridization assay. Anal. Biochem., 306, 314–322 (2002).

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