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Volumn 60, Issue 2, 2005, Pages 123-131

The effect of Zn 2+ on glucose 6-phosphate dehydrogenase activity from Bufo arenarum toad ovary and alfalfa plants

Author keywords

Alfalfa plant; Biomarker; Glucose 6 phosphate dehydrogenase; Toad ovary; Zinc

Indexed keywords

BIOLOGICAL MARKER; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; METAL; PLANT EXTRACT; RINGER SOLUTION; ZINC ION; ZINC;

EID: 8844220591     PISSN: 01476513     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ecoenv.2004.07.008     Document Type: Article
Times cited : (5)

References (32)
  • 1
    • 0032844678 scopus 로고    scopus 로고
    • Exposure and effect monitoring: A critical appraisal of their application
    • A. Aitio, and A. Kallio Exposure and effect monitoring a critical appraisal of their application Toxicol. Lett. 108 1999 137 147
    • (1999) Toxicol. Lett. , vol.108 , pp. 137-147
    • Aitio, A.1    Kallio, A.2
  • 2
    • 0032170104 scopus 로고    scopus 로고
    • Enzyme activity in parotid and mandibular saliva from red kangaroos, Macropus rufus
    • A.M. Beal Enzyme activity in parotid and mandibular saliva from red kangaroos, Macropus rufus Arch. Oral Biol. 43 1998 695 699
    • (1998) Arch. Oral Biol. , vol.43 , pp. 695-699
    • Beal, A.M.1
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0020638768 scopus 로고
    • A rapid affinity chromatography procedure for the isolation of glucose 6-phosphate dehydrogenase from human erythrocytes
    • C.L. Craney, and M.R. Goffredo A rapid affinity chromatography procedure for the isolation of glucose 6-phosphate dehydrogenase from human erythrocytes Anal. Biochem. 128 1983 312 316
    • (1983) Anal. Biochem. , vol.128 , pp. 312-316
    • Craney, C.L.1    Goffredo, M.R.2
  • 7
    • 0018787420 scopus 로고
    • Purification of a new high activity form of glucose 6-phosphate dehydrogenase from rat liver and the effect of enzyme inactivation on its immunochemical reactivity
    • M.L. Dao, J.J. Watson, R. Delaney, and B. Connor Johnson Purification of a new high activity form of glucose 6-phosphate dehydrogenase from rat liver and the effect of enzyme inactivation on its immunochemical reactivity J. Biol. Chem. 254 1979 9441 9447
    • (1979) J. Biol. Chem. , vol.254 , pp. 9441-9447
    • Dao, M.L.1    Watson, J.J.2    Delaney, R.3    Connor Johnson, B.4
  • 8
    • 0031917553 scopus 로고    scopus 로고
    • Meiotic induction in cumulus cell-enclosed mouse oocytes: Involvement of the pentose phosphate pathway
    • S.M. Downs, P.G. Humpherson, and H.J. Leese Meiotic induction in cumulus cell-enclosed mouse oocytes involvement of the pentose phosphate pathway Biol. Reprod. 58 1998 1084 1094
    • (1998) Biol. Reprod. , vol.58 , pp. 1084-1094
    • Downs, S.M.1    Humpherson, P.G.2    Leese, H.J.3
  • 9
    • 0022728292 scopus 로고
    • Purification and properties of the cytoplasmic glucose 6-phosphate dehydrogenase from pea leaves
    • K. Fickenscher, and R. Scheibe Purification and properties of the cytoplasmic glucose 6-phosphate dehydrogenase from pea leaves Arch. Biochem. Biophys. 247 1986 393 402
    • (1986) Arch. Biochem. Biophys. , vol.247 , pp. 393-402
    • Fickenscher, K.1    Scheibe, R.2
  • 11
    • 0027260956 scopus 로고
    • Role of the pentose cycle in oxygen radical-mediated toxicity of the thiol-containing radioprotector dithiothreitol in mammalian cells
    • K.D. Held, S.W. Tuttle, and J.E. Biaglow Role of the pentose cycle in oxygen radical-mediated toxicity of the thiol-containing radioprotector dithiothreitol in mammalian cells Radiat. Res. 134 1993 383 389
    • (1993) Radiat. Res. , vol.134 , pp. 383-389
    • Held, K.D.1    Tuttle, S.W.2    Biaglow, J.E.3
  • 12
    • 0030294736 scopus 로고    scopus 로고
    • The physiology of massive zinc accumulation in the liver of female squirrelfish and its relationship to reproduction
    • C. Hogstrand, N.J. Gassman, B. Popova, C.M. Wood, and P.J. Walsh The physiology of massive zinc accumulation in the liver of female squirrelfish and its relationship to reproduction J. Exp. Biol. 199 1996 2543 2554
    • (1996) J. Exp. Biol. , vol.199 , pp. 2543-2554
    • Hogstrand, C.1    Gassman, N.J.2    Popova, B.3    Wood, C.M.4    Walsh, P.J.5
  • 13
    • 0020772224 scopus 로고
    • Glucose 6-phosphate dehydrogenase isozymes in fish: A comparative study
    • G.M. Kidder Glucose 6-phosphate dehydrogenase isozymes in fish a comparative study J. Exp. Zool. 226 1983 385 390
    • (1983) J. Exp. Zool. , vol.226 , pp. 385-390
    • Kidder, G.M.1
  • 14
    • 0028176627 scopus 로고
    • Glucose 6-phosphate dehydrogenase: A "housekeeping" enzyme subject to tissue-specific regulation by hormones, nutrients and oxidant stress
    • R.F. Kletzien, P.K.W. Harris, and L.A. Foellmi Glucose 6-phosphate dehydrogenase a "housekeeping" enzyme subject to tissue-specific regulation by hormones, nutrients and oxidant stress FASEB J. 8 1994 174 181
    • (1994) FASEB J. , vol.8 , pp. 174-181
    • Kletzien, R.F.1    Harris, P.K.W.2    Foellmi, L.A.3
  • 16
    • 0029096711 scopus 로고
    • Vitellogenin and lipovitelin: Zinc proteins of Xenopus laevis oocytes
    • M. Montorzi, K.H. Falchuk, and B.L. Vallee Vitellogenin and lipovitelin zinc proteins of Xenopus laevis oocytes Biochemistry 34 1995 10,851 10,858
    • (1995) Biochemistry , vol.34 , pp. 10851-10858
    • Montorzi, M.1    Falchuk, K.H.2    Vallee, B.L.3
  • 18
    • 0025765204 scopus 로고
    • Functionally important regions of glucose 6-phosphate dehydrogenase defined by the Saccharomyces cerevisiae enzyme and its differences from the mammalian and insect forms
    • B. Persson, H. Jörnvall, I. Wood, and J. Jeffery Functionally important regions of glucose 6-phosphate dehydrogenase defined by the Saccharomyces cerevisiae enzyme and its differences from the mammalian and insect forms Eur. J. Biochem. 198 1991 485 491
    • (1991) Eur. J. Biochem. , vol.198 , pp. 485-491
    • Persson, B.1    Jörnvall, H.2    Wood, I.3    Jeffery, J.4
  • 19
    • 0345410965 scopus 로고    scopus 로고
    • Mammalian small stress proteins protect against oxidative stress through their ability to increase glucose 6-phosphate dehydrogenase activity and by maintaining optimal cellular detoxifying machinery
    • X. Préville, F. Salvemini, S. Giraud, S. Chaufour, C. Paul, G. Stepien, M.V. Ursini, and A.-P. Arrigo Mammalian small stress proteins protect against oxidative stress through their ability to increase glucose 6-phosphate dehydrogenase activity and by maintaining optimal cellular detoxifying machinery Exp. Cell Res. 247 1999 61 78
    • (1999) Exp. Cell Res. , vol.247 , pp. 61-78
    • Préville, X.1    Salvemini, F.2    Giraud, S.3    Chaufour, S.4    Paul, C.5    Stepien, G.6    Ursini, M.V.7    Arrigo, A.-P.8
  • 20
    • 0030026778 scopus 로고    scopus 로고
    • Correlation between glutathione and stimulation of the pentose phosphate cycle in situ in Chinese hamster ovary cells exposed to hydrogen peroxide
    • E. Przybytkowski, and D.A. Averill-Bates Correlation between glutathione and stimulation of the pentose phosphate cycle in situ in Chinese hamster ovary cells exposed to hydrogen peroxide Arch. Biochem. Biophys. 325 1996 91 98
    • (1996) Arch. Biochem. Biophys. , vol.325 , pp. 91-98
    • Przybytkowski, E.1    Averill-Bates, D.A.2
  • 21
    • 8844246086 scopus 로고    scopus 로고
    • An investigation on low cost, locally available substrates potentially suitable for use in the hardening of tissue-cultured plantlets
    • D. Puchooa, B. Ponnusawmy, and Y.F. Wan Chow Wah An investigation on low cost, locally available substrates potentially suitable for use in the hardening of tissue-cultured plantlets Sci. Technol. Res. J. Univ. Mauritius 4 1999 127 143
    • (1999) Sci. Technol. Res. J. Univ. Mauritius , vol.4 , pp. 127-143
    • Puchooa, D.1    Ponnusawmy, B.2    Wan Chow Wah, Y.F.3
  • 22
    • 0020394659 scopus 로고
    • Regulation of carbohydrate metabolism in microinjected frog oocytes
    • J. Radojkovic, and T. Ureta Regulation of carbohydrate metabolism in microinjected frog oocytes Arch. Biol. Med. Exp. 15 1982 395 405
    • (1982) Arch. Biol. Med. Exp. , vol.15 , pp. 395-405
    • Radojkovic, J.1    Ureta, T.2
  • 23
    • 0033613855 scopus 로고    scopus 로고
    • Enhanced glutathione levels and oxidoresistance mediated by increased glucose 6-phosphate dehydrogenase expression
    • F. Salvemini, A. Franzé, A. Iervolino, S. Filosa, S. Salzano, and M.V. Ursini Enhanced glutathione levels and oxidoresistance mediated by increased glucose 6-phosphate dehydrogenase expression J. Biol. Chem. 274 1999 2750 2757
    • (1999) J. Biol. Chem. , vol.274 , pp. 2750-2757
    • Salvemini, F.1    Franzé, A.2    Iervolino, A.3    Filosa, S.4    Salzano, S.5    Ursini, M.V.6
  • 24
    • 0026431982 scopus 로고
    • The control of oxidant stress at fertilization
    • B.M. Shapiro The control of oxidant stress at fertilization Science 252 1991 533 536
    • (1991) Science , vol.252 , pp. 533-536
    • Shapiro, B.M.1
  • 25
    • 0023959763 scopus 로고
    • Enzyme stimulation upon fertilization is revealed in electrically permeabilized sea urchin eggs
    • R.R. Swezey, and D. Epel Enzyme stimulation upon fertilization is revealed in electrically permeabilized sea urchin eggs Proc. Natl. Acad. Sci. USA 85 1988 812 816
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 812-816
    • Swezey, R.R.1    Epel, D.2
  • 26
    • 0032456846 scopus 로고    scopus 로고
    • Biomarkers in toxicology
    • J.A. Timbrell Biomarkers in toxicology Toxicology 129 1998 1 12
    • (1998) Toxicology , vol.129 , pp. 1-12
    • Timbrell, J.A.1
  • 27
    • 0030957038 scopus 로고    scopus 로고
    • Enhanced expression of glucose 6-phosphate dehydrogenase in human cells sustaining oxidative stress
    • M.V. Ursini, A. Prrella, G. Rosa, S. Salzano, and G. Martini Enhanced expression of glucose 6-phosphate dehydrogenase in human cells sustaining oxidative stress Biochem. J. 323 1997 801 806
    • (1997) Biochem. J. , vol.323 , pp. 801-806
    • Ursini, M.V.1    Prrella, A.2    Rosa, G.3    Salzano, S.4    Martini, G.5
  • 28
    • 0000327566 scopus 로고
    • Glucose 6-phosphate dehydrogenase isozymes of maize leaves
    • V. Valenti, M.A. Stanghellini, and P. Pupillo Glucose 6-phosphate dehydrogenase isozymes of maize leaves Plant Physiol. 75 1984 521 526
    • (1984) Plant Physiol. , vol.75 , pp. 521-526
    • Valenti, V.1    Stanghellini, M.A.2    Pupillo, P.3
  • 29
    • 0027394031 scopus 로고
    • The biochemical basis of zinc physiology
    • B.L. Vallee, and K.H. Falchuk The biochemical basis of zinc physiology Physiol. Rev. 73 1993 79 118
    • (1993) Physiol. Rev. , vol.73 , pp. 79-118
    • Vallee, B.L.1    Falchuk, K.H.2
  • 31
    • 0030822030 scopus 로고    scopus 로고
    • Identification of the cysteine residues involved in redox modification of plant plastidic glucose 6-phosphate dehydrogenase
    • I. Wenderoth, R. Scheibe, and A. von Schaewen Identification of the cysteine residues involved in redox modification of plant plastidic glucose 6-phosphate dehydrogenase J. Biol. Chem. 272 1997 26,985 26,990
    • (1997) J. Biol. Chem. , vol.272 , pp. 26985-26990
    • Wenderoth, I.1    Scheibe, R.2    Von Schaewen, A.3
  • 32
    • 0021016157 scopus 로고
    • Comparative properties of three forms of glucose 6-phosphate dehydrogenase in Drosophila melanogaster
    • J.H. Williamson, and M.M. Bentley Comparative properties of three forms of glucose 6-phosphate dehydrogenase in Drosophila melanogaster Biochem. Genet. 21 1983 1153 1166
    • (1983) Biochem. Genet. , vol.21 , pp. 1153-1166
    • Williamson, J.H.1    Bentley, M.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.