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Volumn 66, Issue 12, 2002, Pages 2587-2593

Mutant Luciferase Enzymes from Fireflies with Increased Resistance to Benzalkonium Chloride

Author keywords

ATP bioluminescence; Benzalkonium chloride; Biomass assay; Firefly luciferase; Hygiene monitoring

Indexed keywords

CRUCIATA; LAMPYRIDAE; LUCIOLA CRUCIATA; LUCIOLA LATERALIS; PHOTINUS; PHOTINUS PYRALIS;

EID: 0037601631     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.66.2587     Document Type: Article
Times cited : (23)

References (31)
  • 1
    • 0014904748 scopus 로고
    • Adenosinetriphosphate (ATP) levels in foods contaminated by bacteria
    • Sharpe, A. N., Woodrow, M. N., and Jackson, A. K., Adenosinetriphosphate (ATP) levels in foods contaminated by bacteria. J. Appl. Bacteriol., 33, 758-767 (1970).
    • (1970) J. Appl. Bacteriol. , vol.33 , pp. 758-767
    • Sharpe, A.N.1    Woodrow, M.N.2    Jackson, A.K.3
  • 2
    • 0014816910 scopus 로고
    • Measurement and significance of adenosine triphosphate in activated sludge
    • Patterson, J. W., Brezonik, P. L., and Putnam, H. D., Measurement and significance of adenosine triphosphate in activated sludge. Environ. Sci. Tech-nol., 4, 569-575 (1970).
    • (1970) Environ. Sci. Tech-Nol. , vol.4 , pp. 569-575
    • Patterson, J.W.1    Brezonik, P.L.2    Putnam, H.D.3
  • 3
    • 0027445196 scopus 로고
    • A study of the use of rapid methods for preservative efficiency testing of pharmaceuticals and cosmetics
    • Connolly, P., Bloomfield, S. F., and Denyer, S. P., A study of the use of rapid methods for preservative efficiency testing of pharmaceuticals and cosmetics. J. Appl. Bacteriol., 75, 456-462 (1993).
    • (1993) J. Appl. Bacteriol. , vol.75 , pp. 456-462
    • Connolly, P.1    Bloomfield, S.F.2    Denyer, S.P.3
  • 4
    • 0024728161 scopus 로고
    • Rapid bacteriological screening of cosmetic raw materials by using bioluminescence
    • Nielsen, P., and van Dellen, E., Rapid bacteriological screening of cosmetic raw materials by using bioluminescence. J. Assoc. Off. Anal. Chem., 72, 708-711 (1989).
    • (1989) J. Assoc. Off. Anal. Chem. , vol.72 , pp. 708-711
    • Nielsen, P.1    Van Dellen, E.2
  • 5
    • 0035921840 scopus 로고    scopus 로고
    • The stowaways
    • Clarke, T., The stowaways. Nature, 413, 247-248 (2001).
    • (2001) Nature , vol.413 , pp. 247-248
    • Clarke, T.1
  • 6
    • 0022987494 scopus 로고
    • Detection of bacteriurea by bioluminescence
    • DeLuca, M. A., and McElroy, W. D., Academic Press, New York, pp
    • Hanna, B. A., Detection of bacteriurea by bioluminescence. In “Methods in enzymology Vol. 133”, eds. DeLuca, M. A., and McElroy, W. D., Academic Press, New York, pp. 22-27 (1986).
    • (1986) Methods in Enzymology Vol. 133 , pp. 22-27
    • Hanna, B.A.1
  • 7
    • 0027768880 scopus 로고
    • Thermostabilization of firefly luciferase by a single amino acid substitution at position 217
    • Kajiyama, N., and Nakano, E., Thermostabilization of firefly luciferase by a single amino acid substitution at position 217. Biochemistry, 32, 13795-13799 (1993).
    • (1993) Biochemistry , vol.32 , pp. 13795-13799
    • Kajiyama, N.1    Nakano, E.2
  • 8
    • 0028454414 scopus 로고
    • Enhancement of thermostability of firefly luciferase from Luciola lateralis by a single amino acid substitution
    • Kajiyama, N., and Nakano, E., Enhancement of thermostability of firefly luciferase from Luciola lateralis by a single amino acid substitution. Biosci. Biotechnol. Biochem., 58, 1170-1171 (1994).
    • (1994) Biosci. Biotechnol. Biochem. , vol.58 , pp. 1170-1171
    • Kajiyama, N.1    Nakano, E.2
  • 9
    • 0029825395 scopus 로고    scopus 로고
    • Improved thermostability of the north American firefly luciferase: Saturation mutagenesis at position 354
    • White, P. J., Squirrell, D. J., Arnaud, P., Lowe, C. R., and Murray, J. A. H., Improved thermostability of the north American firefly luciferase: saturation mutagenesis at position 354. Biochem. J., 319, 343-350 (1996).
    • (1996) Biochem. J. , vol.319 , pp. 343-350
    • White, P.J.1    Squirrell, D.J.2    Arnaud, P.3    Lowe, C.R.4    Murray, J.A.H.5
  • 11
    • 0023016136 scopus 로고
    • Extraction of adenosine triphosphate from microbial and somatic cells
    • DeLuca, M. A., and McEloy, W. D., Academic Press, New York
    • Stanley, P. E., Extraction of adenosine triphosphate from microbial and somatic cells. In “Methods in enzymology Vol. 133”, eds. DeLuca, M. A., and McEloy, W. D., Academic Press, New York, pp. 14-21 (1986).
    • (1986) Methods in Enzymology Vol. 133 , pp. 14-21
    • Stanley, P.E.1
  • 12
    • 0016791330 scopus 로고
    • Comparison of methods for extraction of bacterial adenine nucleotides determined by firefly assay
    • Lundin, A., and Thore, A., Comparison of methods for extraction of bacterial adenine nucleotides determined by firefly assay. Appl. Microbiol., 30, 713-721 (1975).
    • (1975) Appl. Microbiol. , vol.30 , pp. 713-721
    • Lundin, A.1    Thore, A.2
  • 13
    • 0002329925 scopus 로고
    • Extraction and automatic luminometric assay of ATP, ADP and AMP
    • Kricka, L. J., Stanley, P. E., Thorpe, G. H. G., and Whitehead, T. P., Academic Press, London, pp
    • Lundin, A., Extraction and automatic luminometric assay of ATP, ADP and AMP. In “Analytical applications of bioluminescence and chemiluminescence”, eds. Kricka, L. J., Stanley, P. E., Thorpe, G. H. G., and Whitehead, T. P., Academic Press, London, pp. 491-501 (1984).
    • (1984) Analytical Applications of Bioluminescence and Chemiluminescence , pp. 491-501
    • Lundin, A.1
  • 15
    • 0020416456 scopus 로고
    • Continuous flow method for extraction and bioluminescence assay of ATP in baker’s yeast
    • Siro, M., Romar, H., and Lovgren, T., Continuous flow method for extraction and bioluminescence assay of ATP in baker’s yeast. European J. Appl. Microbiol. Biotechnol., 15, 258-264 (1982).
    • (1982) European J. Appl. Microbiol. Biotechnol. , vol.15 , pp. 258-264
    • Siro, M.1    Romar, H.2    Lovgren, T.3
  • 16
  • 18
    • 85010571090 scopus 로고
    • U.S. Patent 5004684 (Apr. 2
    • Simpson, W. J., and Hammond, J. R. M., U.S. Patent 5004684 (Apr. 2, 1991).
    • (1991)
    • Simpson, W.J.1    Hammond, J.R.M.2
  • 19
    • 0002355168 scopus 로고
    • ATP extractants neutralized by cyclodextrins
    • Campbell, A. K., Kricka, L. J., and Stanley, P. E., John Wiley & Sons Ltd., Chichester
    • Lundin, A., Anson, J., and Kau, P., ATP extractants neutralized by cyclodextrins. In “Proceedings of the 8th international symposium on bioluminescence and chemiluminescence”, eds. Campbell, A. K., Kricka, L. J., and Stanley, P. E., John Wiley & Sons Ltd., Chichester, pp. 399-402 (1994).
    • (1994) Proceedings of the 8Th International Symposium on Bioluminescence and Chemiluminescence , pp. 399-402
    • Lundin, A.1    Anson, J.2    Kau, P.3
  • 20
    • 85010571101 scopus 로고    scopus 로고
    • U.S. Patent 5558986 (Sep. 24
    • Lundin, A., U.S. Patent 5558986 (Sep. 24, 1996).
    • (1996)
    • Lundin, A.1
  • 22
    • 0030561209 scopus 로고    scopus 로고
    • Construction of biotinylated firefly luciferase using biotin acceptor peptides
    • Tatsumi, H., Fukuda, S., Kikuchi, M., and Koyama, Y., Construction of biotinylated firefly luciferase using biotin acceptor peptides. Anal. Biochem., 243, 176-180 (1996).
    • (1996) Anal. Biochem. , vol.243 , pp. 176-180
    • Tatsumi, H.1    Fukuda, S.2    Kikuchi, M.3    Koyama, Y.4
  • 23
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., Vieira, J., and Messing, J., Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene, 33, 103-119 (1985).
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 24
    • 0024513933 scopus 로고
    • Random mutagenesis of the gene for the beta-subunit of F1-ATPase from Escherichia coli
    • Kironde, F. A., Parsonage, D., and Senior, A. E., Random mutagenesis of the gene for the beta-subunit of F1-ATPase from Escherichia coli. Biochem. J., 259, 421-426 (1989).
    • (1989) Biochem. J. , vol.259 , pp. 421-426
    • Kironde, F.A.1    Parsonage, D.2    Senior, A.E.3
  • 25
    • 0026560798 scopus 로고
    • Purification and characterization of luciferases from fireflies, Luciola cruciata and Luciola lateralis
    • Kajiyama, N., Masuda, T., Tatsumi, H., and Nakano, E., Purification and characterization of luciferases from fireflies, Luciola cruciata and Luciola lateralis. Biochim. Biophys. Acta, 1120, 228-232 (1992).
    • (1992) Biochim. Biophys. Acta , vol.1120 , pp. 228-232
    • Kajiyama, N.1    Masuda, T.2    Tatsumi, H.3    Nakano, E.4
  • 26
    • 0026717564 scopus 로고
    • Molecular cloning and expression in Escherichia coli of a cDNA clone encoding luciferase of a firefly, Lu-ciola lateralis
    • Tatsumi, H., Kajiyama, N., and Nakano, E., Molecular cloning and expression in Escherichia coli of a cDNA clone encoding luciferase of a firefly, Lu-ciola lateralis. Biochim. Biophys. Acta, 1131, 161-165 (1992).
    • (1992) Biochim. Biophys. Acta , vol.1131 , pp. 161-165
    • Tatsumi, H.1    Kajiyama, N.2    Nakano, E.3
  • 27
    • 0030584662 scopus 로고    scopus 로고
    • Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes
    • Conti, E., Franks, N. P., and Brick, P., Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes. Structure, 4, 287-298 (1996).
    • (1996) Structure , vol.4 , pp. 287-298
    • Conti, E.1    Franks, N.P.2    Brick, P.3
  • 28
    • 0031784872 scopus 로고    scopus 로고
    • Structural basis for the inhibition of firefly luciferase by a general anesthetic
    • Franks, N. P., Jenkins, A., Conti, E., Lieb, W. R., and Brick, P., Structural basis for the inhibition of firefly luciferase by a general anesthetic. Biophys. J., 75, 2205-2211 (1998).
    • (1998) Biophys. J. , vol.75 , pp. 2205-2211
    • Franks, N.P.1    Jenkins, A.2    Conti, E.3    Lieb, W.R.4    Brick, P.5
  • 29
    • 0027587589 scopus 로고
    • Thermostable mutants of kanamycin nucleotidyltransferase are also more stable to proteinase K, urea, detergents, and water-miscible organic solvents
    • Liao, H. H., Thermostable mutants of kanamycin nucleotidyltransferase are also more stable to proteinase K, urea, detergents, and water-miscible organic solvents. Enzyme Microb. Technol., 15, 286-292 (1993).
    • (1993) Enzyme Microb. Technol. , vol.15 , pp. 286-292
    • Liao, H.H.1
  • 30
    • 0032551748 scopus 로고    scopus 로고
    • Improved thermostability of a Bacillus a-amylase by deletion of an arginine-glycine residue is caused by enhanced calcium binding
    • Igarashi, K., Hatada, Y., Ikawa, K., Araki, H., Ozawa, T., Kobayashi, T., Ozaki, K., and Ito, S., Improved thermostability of a Bacillus a-amylase by deletion of an arginine-glycine residue is caused by enhanced calcium binding. Biochem. Biophys. Res. Commun., 248, 372-377 (1998).
    • (1998) Biochem. Biophys. Res. Commun. , vol.248 , pp. 372-377
    • Igarashi, K.1    Hatada, Y.2    Ikawa, K.3    Araki, H.4    Ozawa, T.5    Kobayashi, T.6    Ozaki, K.7    Ito, S.8
  • 31
    • 0031214338 scopus 로고    scopus 로고
    • Enzymatic treatment to eliminate the extracellular ATP for improving the detectability of bacterial intracellular ATP
    • Sakakibara, T., Murakami, S., Hattori, N., Nakajima, M., and Imai, K., Enzymatic treatment to eliminate the extracellular ATP for improving the detectability of bacterial intracellular ATP. Anal. Biochem., 250, 157-161 (1997).
    • (1997) Anal. Biochem. , vol.250 , pp. 157-161
    • Sakakibara, T.1    Murakami, S.2    Hattori, N.3    Nakajima, M.4    Imai, K.5


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