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Volumn 323, Issue 1, 2003, Pages 33-38

Amperometric sensor for glutathione reductase activity determination in erythrocyte hemolysate

Author keywords

Amperometric sensor; Glutathione reductase activity; GSH GSSG ratio

Indexed keywords

BLOOD; ENZYME ACTIVITY; PEPTIDES; SPECTROPHOTOMETRY;

EID: 0242690433     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ab.2003.08.025     Document Type: Article
Times cited : (10)

References (46)
  • 2
    • 0033230043 scopus 로고    scopus 로고
    • Glutathione and its role in celullar functions
    • Sies H. Glutathione and its role in celullar functions. Free Radicals Biol. Med. 27:1999;916-921.
    • (1999) Free Radicals Biol. Med. , vol.27 , pp. 916-921
    • Sies, H.1
  • 3
    • 0033231162 scopus 로고    scopus 로고
    • Biologic and pharmacologic regulation of mammalian glutathione syntesis
    • Griffith O.W. Biologic and pharmacologic regulation of mammalian glutathione syntesis. Free Radicals Biol. Med. 27:1999;922-935.
    • (1999) Free Radicals Biol. Med. , vol.27 , pp. 922-935
    • Griffith, O.W.1
  • 4
    • 0025023848 scopus 로고
    • Biochemical mechanisms for oxygen free radical formation during exercise
    • Sjödin B., Wesling H., Apple S. Biochemical mechanisms for oxygen free radical formation during exercise. Sports Med. 10:1990;236-254.
    • (1990) Sports Med. , vol.10 , pp. 236-254
    • Sjödin, B.1    Wesling, H.2    Apple, S.3
  • 5
    • 0032788956 scopus 로고    scopus 로고
    • Aging and acute exercise enhance free radical generation in rat skeletal muscle
    • Bejma J., Ji L.L. Aging and acute exercise enhance free radical generation in rat skeletal muscle. J. Appl. Physiol. 87:1999;465-470.
    • (1999) J. Appl. Physiol. , vol.87 , pp. 465-470
    • Bejma, J.1    Ji, L.L.2
  • 6
    • 0035143723 scopus 로고    scopus 로고
    • Invited Review: Redox modulation of skeletal muscle contraction: What we know and what we don't
    • Reid M.B. Invited Review: redox modulation of skeletal muscle contraction: What we know and what we don't. J. Appl. Physiol. 90:2001;724-731.
    • (2001) J. Appl. Physiol. , vol.90 , pp. 724-731
    • Reid, M.B.1
  • 7
    • 0027512857 scopus 로고
    • Comparisons of ESR and HPLC methods for the detection of hydroxyl radicals in ischemic/reperfused hearts. A relationship between the genesis of oxygen-free radicals and reperfusion-induced arrhythmias
    • Tosaki A., Bagchi D., Hellegouarch A., Pali T., Cordis G.A., Das D.K. Comparisons of ESR and HPLC methods for the detection of hydroxyl radicals in ischemic/reperfused hearts. A relationship between the genesis of oxygen-free radicals and reperfusion-induced arrhythmias. Biochem. Pharmacol. 45:1983;961-969.
    • (1983) Biochem. Pharmacol. , vol.45 , pp. 961-969
    • Tosaki, A.1    Bagchi, D.2    Hellegouarch, A.3    Pali, T.4    Cordis, G.A.5    Das, D.K.6
  • 9
    • 0024299110 scopus 로고
    • Hypoxic damage generates reactive oxigen species in isolated perfused rat liver
    • Jaeschke H., Smith C.V., Mitchell J.R. Hypoxic damage generates reactive oxigen species in isolated perfused rat liver. Biochem. Biophys. Res. Commun. 150:1988;568-574.
    • (1988) Biochem. Biophys. Res. Commun. , vol.150 , pp. 568-574
    • Jaeschke, H.1    Smith, C.V.2    Mitchell, J.R.3
  • 10
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • Dröge W. Free radicals in the physiological control of cell function. Physiol. Rev. 82:2001;47-96.
    • (2001) Physiol. Rev. , vol.82 , pp. 47-96
    • Dröge, W.1
  • 11
    • 0343963252 scopus 로고    scopus 로고
    • Chemical and biological activity of free radicals scavengers in allergic diseases: A review
    • Matés J.M., Péres-Gómes C., Blanca M. Chemical and biological activity of free radicals scavengers in allergic diseases: a review. Clin. Chim. Acta. 296:2000;1-15.
    • (2000) Clin. Chim. Acta , vol.296 , pp. 1-15
    • Matés, J.M.1    Péres-Gómes, C.2    Blanca, M.3
  • 12
    • 0003536299 scopus 로고    scopus 로고
    • Free Radicals in Biology and Medicine
    • Oxford University Press
    • Halliwell B., Gutteridge J.M.C. Free Radicals in Biology and Medicine. second ed. 1998;Oxford University Press.
    • (1998) second ed.
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 13
    • 0028792111 scopus 로고
    • Lipid peroxidation and antioxidants as biomarkers of tissue damage
    • Gutteridge J.M.C. Lipid peroxidation and antioxidants as biomarkers of tissue damage. Clin. Chem. 41:1995;1819-1828.
    • (1995) Clin. Chem. , vol.41 , pp. 1819-1828
    • Gutteridge, J.M.C.1
  • 14
    • 0025732948 scopus 로고
    • Role of oxidative stress in development of complications in diabetes
    • Baynes J.W. Role of oxidative stress in development of complications in diabetes. Diabetes. 40:1991;405-412.
    • (1991) Diabetes , vol.40 , pp. 405-412
    • Baynes, J.W.1
  • 15
    • 0027279232 scopus 로고
    • Diabetes mellitus and free radicals. Free radicals, transition metals and oxidative stress in the aetiology of diabetes mellitus and complications
    • Wolff S.P. Diabetes mellitus and free radicals. Free radicals, transition metals and oxidative stress in the aetiology of diabetes mellitus and complications. Br. Med. Bull. 49:1993;642-652.
    • (1993) Br. Med. Bull. , vol.49 , pp. 642-652
    • Wolff, S.P.1
  • 16
    • 0036797684 scopus 로고    scopus 로고
    • Effect of oxidative stress on glutathione pathway in red cells from patients with insulin-dependent diabetes mellitus
    • Dincer Y., Akcay T., Alademir Z., Ilkova H. Effect of oxidative stress on glutathione pathway in red cells from patients with insulin-dependent diabetes mellitus. Metabolism. 51:2002;1360-1362.
    • (2002) Metabolism , vol.51 , pp. 1360-1362
    • Dincer, Y.1    Akcay, T.2    Alademir, Z.3    Ilkova, H.4
  • 17
    • 0036746683 scopus 로고    scopus 로고
    • Protective effects of quercitin on ultraviolet A light-induced oxidative stress in the blood of rat
    • Kahraman A., Inal M.E. Protective effects of quercitin on ultraviolet A light-induced oxidative stress in the blood of rat. J. Appl. Toxicol. 22:2002;303-309.
    • (2002) J. Appl. Toxicol. , vol.22 , pp. 303-309
    • Kahraman, A.1    Inal, M.E.2
  • 18
    • 0036190993 scopus 로고    scopus 로고
    • Enhanced heme oxygenase activity increases the antioxidant defense capacity of guinea pig liver upon cobalt chlorid loading: Comparison with rat liver
    • Christova T.V., Duridanova D.V., Setchenska M.S. Enhanced heme oxygenase activity increases the antioxidant defense capacity of guinea pig liver upon cobalt chlorid loading: comparison with rat liver. Comp. Biochem. Physiol. C. Toxicol. Pharmacol. 131:2002;177-184.
    • (2002) Comp. Biochem. Physiol. C. Toxicol. Pharmacol. , vol.131 , pp. 177-184
    • Christova, T.V.1    Duridanova, D.V.2    Setchenska, M.S.3
  • 19
    • 0036366982 scopus 로고    scopus 로고
    • Lipoic acid in combination with a chelator ameliorates lead-induced peroxidative damages in rat kidney
    • Sivaprasad R., Nagaraf M., Varalakshimi P. Lipoic acid in combination with a chelator ameliorates lead-induced peroxidative damages in rat kidney. Arch. Toxicol. 76:2002;437-441.
    • (2002) Arch. Toxicol. , vol.76 , pp. 437-441
    • Sivaprasad, R.1    Nagaraf, M.2    Varalakshimi, P.3
  • 20
    • 0023846309 scopus 로고
    • Free radical chemistry: Relationship to exercise
    • Jenkins R.R. Free radical chemistry: relationship to exercise. Sports Med. 5:1988;156-170.
    • (1988) Sports Med. , vol.5 , pp. 156-170
    • Jenkins, R.R.1
  • 21
    • 0022378881 scopus 로고
    • Effect of exercise training on antioxidant status enzymes and cardiotoxity of doxrubicin
    • Kanter M.M., Hamlin R.L., Unverferth D.V., Davies M.W., Merola A.J. Effect of exercise training on antioxidant status enzymes and cardiotoxity of doxrubicin. J. Appl. Physiol. 59:1985;1298-1303.
    • (1985) J. Appl. Physiol. , vol.59 , pp. 1298-1303
    • Kanter, M.M.1    Hamlin, R.L.2    Unverferth, D.V.3    Davies, M.W.4    Merola, A.J.5
  • 22
    • 0029022127 scopus 로고
    • Oxidants and antioxidant in exercise
    • Sen C.K. Oxidants and antioxidant in exercise. J. Appl. Physiol. 79:1995;675-686.
    • (1995) J. Appl. Physiol. , vol.79 , pp. 675-686
    • Sen, C.K.1
  • 23
    • 0027474539 scopus 로고
    • Blood glutathione status during exercise: Effect of carbohydrate supplementation
    • Ji L.L., Katz A., Fu R., Griffiths M., Spencer M. Blood glutathione status during exercise: effect of carbohydrate supplementation. J. Appl. Physiol. 74:1993;788-792.
    • (1993) J. Appl. Physiol. , vol.74 , pp. 788-792
    • Ji, L.L.1    Katz, A.2    Fu, R.3    Griffiths, M.4    Spencer, M.5
  • 24
    • 0031737829 scopus 로고    scopus 로고
    • Radical species in inflammation and overtraining
    • Tiidus P.M. Radical species in inflammation and overtraining. Can. J. Physiol. Pharmacol. 76:1998;533-538.
    • (1998) Can. J. Physiol. Pharmacol. , vol.76 , pp. 533-538
    • Tiidus, P.M.1
  • 25
    • 0034812632 scopus 로고    scopus 로고
    • Exercise and oxidative stress: Significance and antioxidantes with reference to inflamatory muscular and systemic stress
    • Konig D., Wagner R.H., Elmadfa I., Berger A. Exercise and oxidative stress: significance and antioxidantes with reference to inflamatory muscular and systemic stress. Exerc. Immun. Rev. 7:2001;108-133.
    • (2001) Exerc. Immun. Rev. , vol.7 , pp. 108-133
    • Konig, D.1    Wagner, R.H.2    Elmadfa, I.3    Berger, A.4
  • 28
    • 0024595407 scopus 로고
    • Catalase and glutathione peroxidase are equally active in detoxification of hidrogen peroxide in human erytrocytes
    • Gaetani G.F., Galiano S., Canefra L., Ferraris A.M., Kirkman H.N. Catalase and glutathione peroxidase are equally active in detoxification of hidrogen peroxide in human erytrocytes. Blood. 73:1989;334-339.
    • (1989) Blood , vol.73 , pp. 334-339
    • Gaetani, G.F.1    Galiano, S.2    Canefra, L.3    Ferraris, A.M.4    Kirkman, H.N.5
  • 29
    • 0028176627 scopus 로고
    • Glucose-6-phosphate dehydrogenase: A "housekeeping" enzyme subject to tissue-specific regulation by hormones, nutrients and oxidative stress
    • Kletzien R.F., Harris P.K., Foellni L.A. Glucose-6-phosphate dehydrogenase: a "housekeeping" enzyme subject to tissue-specific regulation by hormones, nutrients and oxidative stress. FASEB J. 8:1994;174-181.
    • (1994) FASEB J. , vol.8 , pp. 174-181
    • Kletzien, R.F.1    Harris, P.K.2    Foellni, L.A.3
  • 30
    • 0019882046 scopus 로고
    • Three-diementional struture of glutathione reductase at 2 A resolution
    • Thieme R., Pai E.P., Schirmer R.H., Schulz G.E. Three-diementional struture of glutathione reductase at 2 A resolution. J. Mol. Biol. 152:1981;763-782.
    • (1981) J. Mol. Biol. , vol.152 , pp. 763-782
    • Thieme, R.1    Pai, E.P.2    Schirmer, R.H.3    Schulz, G.E.4
  • 31
    • 0023173876 scopus 로고
    • Mechanism of action of glutathione-dependent enzymes
    • K.T. Douglas, Mechanism of action of glutathione-dependent enzymes, Adv. Enzymol. Relat Areas Mol. Biol. 59 (1987) (2001) 103-167.
    • (1987) Adv. Enzymol. Relat Areas Mol. Biol. , vol.59 , pp. 103-167
    • Douglas, K.T.1
  • 32
    • 0022272481 scopus 로고
    • Glutathione peroxidase
    • Mannervik B. Glutathione peroxidase. Methods Enzymol. 113:1985;490-495.
    • (1985) Methods Enzymol. , vol.113 , pp. 490-495
    • Mannervik, B.1
  • 33
    • 0023769999 scopus 로고
    • Micromethods in single muscle fibers: 2. Determination of glutathione reductase and glutathione peroxidase
    • Austin L., Arthur H., De Niese M., Gurunsinghe A., Baker M.S. Micromethods in single muscle fibers: 2. Determination of glutathione reductase and glutathione peroxidase. Anal. Biochem. 174:1988;575-579.
    • (1988) Anal. Biochem. , vol.174 , pp. 575-579
    • Austin, L.1    Arthur, H.2    De Niese, M.3    Gurunsinghe, A.4    Baker, M.S.5
  • 35
  • 36
    • 0242670016 scopus 로고    scopus 로고
    • Ellman's-reagent-mediated regeneration of trypanothione in situ: Substrate-economical microplate and time-dependent inhibition assays for trypanothione reductase
    • Hamilton C.J., Saravanamuthu A., Eggleston I.M., Fairlamb A.H. Ellman's-reagent-mediated regeneration of trypanothione in situ: substrate-economical microplate and time-dependent inhibition assays for trypanothione reductase. Biochem. J. 369:2003;529-537.
    • (2003) Biochem. J. , vol.369 , pp. 529-537
    • Hamilton, C.J.1    Saravanamuthu, A.2    Eggleston, I.M.3    Fairlamb, A.H.4
  • 38
    • 0025979272 scopus 로고
    • Human jejunal glutathione reductase: Purification and evaluation of NADPH- and glutathione induced changes in redox state
    • Ogus H., Ozer N. Human jejunal glutathione reductase: purification and evaluation of NADPH- and glutathione induced changes in redox state. Biochem. Med. Metab. Biol. 45:1991;65-73.
    • (1991) Biochem. Med. Metab. Biol. , vol.45 , pp. 65-73
    • Ogus, H.1    Ozer, N.2
  • 39
    • 0024421234 scopus 로고
    • Substrate binding and catalysis by glutathione-reductase as derived from refined enzyme-substrate crystal-structures at 2 A resolution
    • Karplus P.A., Schulz G.E. Substrate binding and catalysis by glutathione-reductase as derived from refined enzyme-substrate crystal-structures at 2 A resolution. J. Mol. Biol. 210:1989;163-180.
    • (1989) J. Mol. Biol. , vol.210 , pp. 163-180
    • Karplus, P.A.1    Schulz, G.E.2
  • 40
    • 0031662696 scopus 로고    scopus 로고
    • Inhibitors of glutathione reductase as potential antimalarial drugs. Kinetic cooperativity and effect of dimethyl sulphoxide on inhibition kinetics
    • Luond R.M., Mckie J.H., Douglas K.T., Descombe M.J., Vale J. Inhibitors of glutathione reductase as potential antimalarial drugs. Kinetic cooperativity and effect of dimethyl sulphoxide on inhibition kinetics. J. Enzyme Inhib. 13:1998;327-345.
    • (1998) J. Enzyme Inhib. , vol.13 , pp. 327-345
    • Luond, R.M.1    Mckie, J.H.2    Douglas, K.T.3    Descombe, M.J.4    Vale, J.5
  • 42
    • 0037217858 scopus 로고    scopus 로고
    • Mitochondrial DNA replication, nucloside reverse-transcriptase inhibitors, and AIDS cardiomyopathy
    • Lewis W. Mitochondrial DNA replication, nucloside reverse-transcriptase inhibitors, and AIDS cardiomyopathy. Prog. Cardiovasc. Dis. 45:2003;305-318.
    • (2003) Prog. Cardiovasc. Dis. , vol.45 , pp. 305-318
    • Lewis, W.1
  • 45
    • 0035383102 scopus 로고    scopus 로고
    • Exposure to hyperoxia in diving and hyperbaric medicine, effects on blood cell counts and serum ferritin
    • Thorsen E., Haave H., Hofso D., Ulvik R.J. Exposure to hyperoxia in diving and hyperbaric medicine, effects on blood cell counts and serum ferritin. Undersea Hyperb. Med. 28:2001;57-62.
    • (2001) Undersea Hyperb. Med. , vol.28 , pp. 57-62
    • Thorsen, E.1    Haave, H.2    Hofso, D.3    Ulvik, R.J.4
  • 46
    • 0031255704 scopus 로고    scopus 로고
    • Muscle fatigue and induction of stress protein genes: A dual function of reactive oxygen species
    • Essig D.A., Nosek T.A. Muscle fatigue and induction of stress protein genes: a dual function of reactive oxygen species. Can. J. Appl. Physiol. 22:1997;409-428.
    • (1997) Can. J. Appl. Physiol. , vol.22 , pp. 409-428
    • Essig, D.A.1    Nosek, T.A.2


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