메뉴 건너뛰기




Volumn 42, Issue 12, 1996, Pages 1197-1202

Induction of superoxide dismutase synthesis in Humicola lutea 110 by pentachlorophenol

Author keywords

fungi; Humicola lutea; induction; pentachlorophenol; superoxide; superoxide dismutase

Indexed keywords

PENTACHLOROPHENOL; SUPEROXIDE DISMUTASE;

EID: 0030497627     PISSN: 00084166     EISSN: None     Source Type: Journal    
DOI: 10.1139/m96-154     Document Type: Article
Times cited : (7)

References (34)
  • 1
    • 0009752881 scopus 로고
    • Humicola lutea 110 - Argon-laser mutant, producer of superoxide dismutase and acid proteinase
    • Angelova, M., Genova, L., Djerova, A., Slokoska, L., and Sheremetska, P. 1993a. Humicola lutea 110 - Argon-laser mutant, producer of superoxide dismutase and acid proteinase. C. R. Acad. Bulg. Sci. 46: 77-80.
    • (1993) C. R. Acad. Bulg. Sci. , vol.46 , pp. 77-80
    • Angelova, M.1    Genova, L.2    Djerova, A.3    Slokoska, L.4    Sheremetska, P.5
  • 2
    • 0343772894 scopus 로고
    • Comparative studies of SOD and acid proteinase synthesis in argon-laser mutant Humicola lutea 110 and parent strain Humicola lutea 72
    • Angelova, M., Genova, L., Djerova, A., Slokoska, L., Sheremetska, P., and Pashova, S. 1993b. Comparative studies of SOD and acid proteinase synthesis in argon-laser mutant Humicola lutea 110 and parent strain Humicola lutea 72. C. R. Acad. Bulg. Sci. 46: 81-84.
    • (1993) C. R. Acad. Bulg. Sci. , vol.46 , pp. 81-84
    • Angelova, M.1    Genova, L.2    Djerova, A.3    Slokoska, L.4    Sheremetska, P.5    Pashova, S.6
  • 3
    • 21844498401 scopus 로고
    • Effects of redox active compounds on the superoxide dismutase synthesis in fungal strain Humicola lutea 110
    • Angelova, M., Genova, L., Pashova, S., and Slokoska, L. 1995a. Effects of redox active compounds on the superoxide dismutase synthesis in fungal strain Humicola lutea 110. Oxid. Commun. 18: 420-426.
    • (1995) Oxid. Commun. , vol.18 , pp. 420-426
    • Angelova, M.1    Genova, L.2    Pashova, S.3    Slokoska, L.4
  • 4
    • 0028880549 scopus 로고
    • Effect of glucose on the superoxide dismutase production in fungal strain Humicola lutea
    • Angelova, M., Genova, L., Slokoska, L., and Pashova, S. 1995b. Effect of glucose on the superoxide dismutase production in fungal strain Humicola lutea. Can. J. Microbiol. 41: 978-983.
    • (1995) Can. J. Microbiol. , vol.41 , pp. 978-983
    • Angelova, M.1    Genova, L.2    Slokoska, L.3    Pashova, S.4
  • 5
    • 8044226067 scopus 로고
    • Involvement of active forms of oxygen in the mechanism of ferulic acid toxicity
    • Averjanov, A., and Lapikova, V. 1985. Involvement of active forms of oxygen in the mechanism of ferulic acid toxicity. Izv. Akad. Nauk. Ser. Biol. 4: 521-527.
    • (1985) Izv. Akad. Nauk. Ser. Biol. , vol.4 , pp. 521-527
    • Averjanov, A.1    Lapikova, V.2
  • 6
    • 0015153416 scopus 로고
    • Superoxide dismutase: Improved assays and an assay applicable to polyacrylamide gels
    • Beauchamp, C., and Fridovich, I. 1971. Superoxide dismutase: improved assays and an assay applicable to polyacrylamide gels. Anal. Biochem. 44: 276-287.
    • (1971) Anal. Biochem. , vol.44 , pp. 276-287
    • Beauchamp, C.1    Fridovich, I.2
  • 7
    • 41049100518 scopus 로고
    • A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase
    • Beers, R.F., and Sizer, I. W. 1952. A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J. Biol. Chem. 195: 133-140.
    • (1952) J. Biol. Chem. , vol.195 , pp. 133-140
    • Beers, R.F.1    Sizer, I.W.2
  • 8
    • 0028054245 scopus 로고
    • Induction of the iron-containing superoxide dismutase in Entamoeba histolytica by a superoxide anion-generating system or by iron chelation
    • Bruchhaus, I., and Tannich, E. 1994. Induction of the iron-containing superoxide dismutase in Entamoeba histolytica by a superoxide anion-generating system or by iron chelation. Mol. Biochem. Parasitol. 67: 281-288.
    • (1994) Mol. Biochem. Parasitol. , vol.67 , pp. 281-288
    • Bruchhaus, I.1    Tannich, E.2
  • 9
    • 84912519741 scopus 로고
    • Mechanism for superoxide and peroxide production from dioxygen and hemoglobins
    • Edited by G. Cohen and R.A. Greenwald. Elsevier Science Publishing Co., Inc., New York
    • Caugher, W.S., and Kawanigshi, S. 1983. Mechanism for superoxide and peroxide production from dioxygen and hemoglobins. In Oxyradicals and their scavenger systems. Vol. 1. Molecular aspects. Edited by G. Cohen and R.A. Greenwald. Elsevier Science Publishing Co., Inc., New York. pp. 105-110.
    • (1983) Oxyradicals and Their Scavenger Systems. Vol. 1. Molecular Aspects , vol.1 , pp. 105-110
    • Caugher, W.S.1    Kawanigshi, S.2
  • 10
    • 78651153791 scopus 로고
    • Disc gel electrophoresis
    • Davis, B.J. 1964. Disc gel electrophoresis. Ann. N.Y. Acad. Sci. 121: 404-427.
    • (1964) Ann. N.Y. Acad. Sci. , vol.121 , pp. 404-427
    • Davis, B.J.1
  • 11
    • 0025986138 scopus 로고
    • Regulation of sod genes in Esherichia coli: Relevance to superoxide dismutase function
    • Fee, J.A. 1991. Regulation of sod genes in Esherichia coli: relevance to superoxide dismutase function. Mol. Microbiol. 5: 2599-2610.
    • (1991) Mol. Microbiol. , vol.5 , pp. 2599-2610
    • Fee, J.A.1
  • 13
    • 0027378686 scopus 로고
    • Mechanism of cytotoxicity of paraquat. I. NADH oxidation and paraquat radical formation via complex I
    • Fukushima, T., Yamada, K., Shiwaku, K., and Yamane, Y. 1993. Mechanism of cytotoxicity of paraquat. I. NADH oxidation and paraquat radical formation via complex I. Exp. Toxicol. Pathol. 45: 345-349.
    • (1993) Exp. Toxicol. Pathol. , vol.45 , pp. 345-349
    • Fukushima, T.1    Yamada, K.2    Shiwaku, K.3    Yamane, Y.4
  • 14
    • 8044235011 scopus 로고
    • Generation of superoxide anion radicals by autooxidation of pentachlorophenol
    • Genova, L., Pashova, S., Slokoska, L., and Angelova, M. 1995. Generation of superoxide anion radicals by autooxidation of pentachlorophenol. C. R. Acad. Bulg. Sci. 48: 71-73.
    • (1995) C. R. Acad. Bulg. Sci. , vol.48 , pp. 71-73
    • Genova, L.1    Pashova, S.2    Slokoska, L.3    Angelova, M.4
  • 15
    • 0026634285 scopus 로고
    • Regulation of antioxidant enzymes
    • Harris, E.D. 1992. Regulation of antioxidant enzymes. FASEB J. 6: 2675-2683.
    • (1992) FASEB J. , vol.6 , pp. 2675-2683
    • Harris, E.D.1
  • 16
    • 0024330563 scopus 로고
    • Microbial superoxide dismutases
    • Hassan, H.M. 1989. Microbial superoxide dismutases. Adv. Genet. 26: 65-97.
    • (1989) Adv. Genet. , vol.26 , pp. 65-97
    • Hassan, H.M.1
  • 17
    • 0017343504 scopus 로고
    • Enzymatic defences against the toxicity of oxygen and of streptonigrin in Escherichia coli
    • Hassan, H.M., and Fridovich, I. 1977a. Enzymatic defences against the toxicity of oxygen and of streptonigrin in Escherichia coli. J. Bacteriol. 129: 1574-1583.
    • (1977) J. Bacteriol. , vol.129 , pp. 1574-1583
    • Hassan, H.M.1    Fridovich, I.2
  • 18
    • 0017760575 scopus 로고
    • Regulation of the synthesis of superoxide dismutases in Escherichia coli. Induction by methyl viologen
    • Hassan, H.M., and Fridovich, I. 1977b. Regulation of the synthesis of superoxide dismutases in Escherichia coli. Induction by methyl viologen. J. Biol. Chem. 252: 7667-7672.
    • (1977) J. Biol. Chem. , vol.252 , pp. 7667-7672
    • Hassan, H.M.1    Fridovich, I.2
  • 19
    • 0018666716 scopus 로고
    • Intracellular production of superoxide radical and hydrogen peroxide by redox active compounds
    • Hassan, H.M., and Fridovich, I. 1979. Intracellular production of superoxide radical and hydrogen peroxide by redox active compounds. Arch. Biochem. Biophys. 196: 385-395.
    • (1979) Arch. Biochem. Biophys. , vol.196 , pp. 385-395
    • Hassan, H.M.1    Fridovich, I.2
  • 20
    • 3042762784 scopus 로고
    • Regulation of the biosynthesis of superoxide dismutase in prokaryotes
    • Edited by G. Rotilio, Elsevier Science Publishers. New York
    • Hassan, H M., and Moody, C. S. 1986. Regulation of the biosynthesis of superoxide dismutase in prokaryotes. In Superoxide and superoxide dismutase in chemistry, biology and medicine. Edited by G. Rotilio, Elsevier Science Publishers. New York. pp. 274-279.
    • (1986) Superoxide and Superoxide Dismutase in Chemistry, Biology and Medicine , pp. 274-279
    • Hassan, H.M.1    Moody, C.S.2
  • 21
    • 0028031008 scopus 로고
    • Roles of manganese and iron in the regulation of the biosynthesis of manganese-superoxide dismutase in Escherichia coli
    • Hassan, H.M., and Schrum, L.W. 1994. Roles of manganese and iron in the regulation of the biosynthesis of manganese-superoxide dismutase in Escherichia coli. FEMS Microbiol. Rev. 14: 315-324.
    • (1994) FEMS Microbiol. Rev. , vol.14 , pp. 315-324
    • Hassan, H.M.1    Schrum, L.W.2
  • 22
    • 0019274222 scopus 로고
    • Developmental regulation of laccase levels in Aspergillus nidulans
    • Law, D.J., and Timberlake, W.E. 1980. Developmental regulation of laccase levels in Aspergillus nidulans. J. Bacteriol. 144: 509-517.
    • (1980) J. Bacteriol. , vol.144 , pp. 509-517
    • Law, D.J.1    Timberlake, W.E.2
  • 24
    • 34249967141 scopus 로고
    • Catabolite repression of the synthesis of inducible polygalacturonase and pectinesterase by Aspergillus niger sp.
    • Maldonado, M. C., Strasser de Saad, A. M., and Callieri, D. 1989. Catabolite repression of the synthesis of inducible polygalacturonase and pectinesterase by Aspergillus niger sp. Curr. Microbiol. 18: 303-306.
    • (1989) Curr. Microbiol. , vol.18 , pp. 303-306
    • Maldonado, M.C.1    Strasser De Saad, A.M.2    Callieri, D.3
  • 25
    • 0016272750 scopus 로고
    • Involvement of the superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase
    • Marklund, S., and Marklund, C. 1974. Involvement of the superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase. Eur. J. Biochem. 47: 469-475.
    • (1974) Eur. J. Biochem. , vol.47 , pp. 469-475
    • Marklund, S.1    Marklund, C.2
  • 26
    • 0016699018 scopus 로고
    • Generation of superoxide anions by leucocytes treated with cytochalasin E
    • Nakagawara, A., and Minakami, S. 1975. Generation of superoxide anions by leucocytes treated with cytochalasin E. Biochem. Biophys. Res. Commun. 64: 760-767.
    • (1975) Biochem. Biophys. Res. Commun. , vol.64 , pp. 760-767
    • Nakagawara, A.1    Minakami, S.2
  • 27
    • 0025597981 scopus 로고
    • Anaerobic biosynthesis of Mn-containing superoxide dismutase in Escherichia coli
    • Privalle, C., and Fridovich, I. 1990. Anaerobic biosynthesis of Mn-containing superoxide dismutase in Escherichia coli. J. Biol. Chem. 265: 21 966-21 970.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21966-21970
    • Privalle, C.1    Fridovich, I.2
  • 28
    • 0021924999 scopus 로고
    • Induction of superoxide dismutase in Escherichia coli by metal chelators
    • Pugh, S. Y., and Fridovich, I. 1985. Induction of superoxide dismutase in Escherichia coli by metal chelators. J. Bacteriol. 162: 196-202.
    • (1985) J. Bacteriol. , vol.162 , pp. 196-202
    • Pugh, S.Y.1    Fridovich, I.2
  • 29
    • 1842785754 scopus 로고
    • A method for determination of DNA, RNA and phosphoproteins in animal tissues
    • Tokyo
    • Schmidt, G., and Thanchauser, S.J. 1945. A method for determination of DNA, RNA and phosphoproteins in animal tissues. J. Biochem. (Tokyo), 161: 83-88.
    • (1945) J. Biochem. , vol.161 , pp. 83-88
    • Schmidt, G.1    Thanchauser, S.J.2
  • 31
    • 0025237829 scopus 로고
    • Toxicities of dicyanobenzofurazans with formation of superoxide in Escherichia coli
    • Takabatake, T., Hasegawa, M., Nagano, T., and Hirobe, M. 1990. Toxicities of dicyanobenzofurazans with formation of superoxide in Escherichia coli. Chem. Pharm. Bull. 138: 128-132.
    • (1990) Chem. Pharm. Bull. , vol.138 , pp. 128-132
    • Takabatake, T.1    Hasegawa, M.2    Nagano, T.3    Hirobe, M.4
  • 32
    • 0002554499 scopus 로고
    • Regulation and protective role of the microbial superoxide dismutase
    • Edited by J.G. Scandalios. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Touati, D. 1992. Regulation and protective role of the microbial superoxide dismutase. In Molecular biology of free radical scavenging systems. Edited by J.G. Scandalios. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y. pp. 231-261.
    • (1992) Molecular Biology of Free Radical Scavenging Systems , pp. 231-261
    • Touati, D.1
  • 33
    • 0017409903 scopus 로고
    • Rapid induction of α-amylase by nongrowing mycelia of Aspergillus oryzae
    • Yabuki, M., Ono, N., Hoshino, K., and Fukui, S. 1977. Rapid induction of α-amylase by nongrowing mycelia of Aspergillus oryzae. Appl. Environ. Microbiol. 34: 1-6.
    • (1977) Appl. Environ. Microbiol. , vol.34 , pp. 1-6
    • Yabuki, M.1    Ono, N.2    Hoshino, K.3    Fukui, S.4
  • 34
    • 0019253469 scopus 로고
    • Localization of secreted enzyme-induced repression of its synthesis by the cells
    • Moscow
    • Yurkevich, V.V., Kozyreva, G.T., and Kovaleva, N.S. 1980. Localization of secreted enzyme-induced repression of its synthesis by the cells. Biokimiya (Moscow), 45: 2115-2120.
    • (1980) Biokimiya , vol.45 , pp. 2115-2120
    • Yurkevich, V.V.1    Kozyreva, G.T.2    Kovaleva, N.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.