Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or... – Involving luciferase
Reexamination Certificate
2008-07-08
2008-07-08
Weber, Jon P (Department: 1657)
Chemistry: molecular biology and microbiology
Measuring or testing process involving enzymes or...
Involving luciferase
Reexamination Certificate
active
07396655
ABSTRACT:
Methods for enhancing luminescence of a luciferase (BFP-aq) with fluorescence activity derived from a calcium-binding photoprotein are provided. To a luciferase solution with fluorescence activity that contains an apoprotein, a calcium-binding photoprotein, which is constituted such that a coelenteramide or an analog thereof is coordinated inside, a coelenterazine that is the luminescent substrate of the luciferase or an analog thereof and a compound (e.g., imidazole etc.) having the function of removing an —NH-proton of the pyrazine ring of the imidazopyrazine skeleton in the coelenterazine or the analog thereof are added.
REFERENCES:
patent: 5360728 (1994-11-01), Prasher
patent: 5824472 (1998-10-01), Betlach et al.
patent: 2004/0235078 (2004-11-01), Rosen et al.
patent: 2005/0054838 (2005-03-01), Otsuka et al.
patent: 1 666 488 (2006-06-01), None
patent: 1 666 488 (2006-07-01), None
patent: 61-135586 (1986-06-01), None
patent: 1-132397 (1989-05-01), None
patent: 3162480 (1991-07-01), None
patent: 3167288 (1991-07-01), None
patent: 2001-270899 (2001-10-01), None
patent: 2004-035449 (2004-02-01), None
patent: 2004-156017 (2004-03-01), None
patent: 2006055082 (2006-03-01), None
patent: WO 87/05937 (1987-10-01), None
patent: WO 00/29603 (2000-05-01), None
patent: WO 03/054163 (2003-07-01), None
patent: WO 03/060063 (2003-07-01), None
patent: WO 03/082904 (2003-10-01), None
patent: WO2005/014633 (2005-02-01), None
Huang et al. Identification and Characterization of a Catalytic Base in Bacterial Luciferase by Chemical Rescue ofa Dark Mutant; Biochemistry, vol. 36, No. 48 (1997) pp. 14609-14615.
Inouye et al. Imidazole-Assisted Catalysis of Luminescence Reaction in Blue Fluorescent Protein From the Photoprotein Aequorin; Biochemical and Biophysical Research Communications, vol. 354 (2007) pp. 650-655.
Tsuji et al. “Bioluminescence Reaction Catalyzed by Membrane-Bound Luciferase in the ‘Firefly Squid,’ Watasenia Scintillans,”Biochimica et Biophsica Acta 1564: 189-197 (2002).
Deng et al., “Crystal Structure of a Ca2+ -discharged Photoprotein,”J. Biological Chemistry, 279 (32): 33647-33652 (Aug. 6, 2004).
Inouye, “Fusions to Imidazopyrazinone-Type Luciferases and Aequorin as Reporters,”Methods in Enzymology, 326: 165-174 (2000).
Shimomura et al., “The relative rate of aequorin regeneration from apoaequorin and coelenterazine analogues,”Biochem J., 296: 549-551 (1993).
Shimomura et al., “Recombinant aequorin and recombinant semi-synthetic aequorins,”Biochem J., 270: 309-312 (1990).
Shimomura et al., “Light-emitting properties of recombinant semi-synthetic aequorins and recombinant fluorescein-conjugated aequorin for measuring cellular calcium,”Cell Calcium, 14: 373-378 (1993).
Vysotski et al., “Ca2+ -Regulated Photoproteins: Structural Insight into the Bioluminescence Mechanism,”Acc. Chem. Res., 37 (6): 405-415 (2004).
Bondar et al., “Cadmium-Induced Luminescence of Recombinant Photoprotein Obelin,”Biochimica et Biophysica Acta, 1231: 29-32 (1995).
Deng et al., “Structural Basis for the Emission of Violet Bioluminescence from a W92F Obelin Mutant,”FEBS Letters, 506(3): 281-285 (Oct. 12, 2001).
Head et al., “The Crystal Structure of the Photoprotein Aequorin at 2.3 A Resolution,”Nature, 405(6784): 372-376 (May 18, 2000).
Inouye et al., “Cloning and Sequence Analysis of cDNA for the Luminescent Protein Aequorin,”Proc. Natl. Acad. Sci. USA, 82(10): 3154-3158 (May 1985).
Stephenson et al., “Studies on the Luminescent Response of the Ca2+-Activated Photoprotein, Obelin,”Biochimica et Biophysica Acta, 678: 65-75 (1981).
Jena Bioscience, “Crystallization screens—JBScreen PEG/Salt, 2004,” available at http://www.jenabioscience.com/index.php/5314c472c8c9389eb2e90848aba236cd/1/catalog/1005 (Retrieved Feb. 3, 2007).
The Patent Office: Patents Directorate, Search Report for Application No. GB0608514.6, dated Mar. 12, 2007.
The Patent Office Patents Directorate, Search Report for Application No. GB0608514.6, dated Aug. 18, 2007.
Inouye, et al. “Blue Fluorescent Protein from the Calcium-Sensitive Photoprotein Aequorin: Catalytic Properties for the Oxidation of Coelenterazine as an Oxygenase,”FEBS Letters, 580: 1977-1982 (2006).
Inouye et al., “The Use of Renilla Luciferase, Oplophorus Luciferase, and Apoaequorin as Bioluminescent Reporter Protein in the Presence of Coelenterazine Analogues as Substrate,”Biochemical and Biophysical Research Communications, 233(2): 349-353 (Apr. 17, 1997).
Inouye, “Blue Fluorescent Protein from the Calcium-Sensitive Photoprotein Aequorin is a Heat Resistant Enzyme, Catalyzing the Oxidation of Coelenterazine,”FEBS Letters, 577(1-2):105-110 (2004).
Inouye Satoshi
Sasaki Satoko
Chisso Corporation
Leydig , Voit & Mayer, Ltd.
Martin Paul C.
Weber Jon P
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