메뉴 건너뛰기




Volumn 50, Issue 1, 1999, Pages 75-87

Effects of nitroglycerin on energy metabolism of rat reticulocytes

Author keywords

Energy metabolism; Glycolysis; Nitric oxide; Nitroglycerin; Oxidative phosphorylation; Rat reticulocytes

Indexed keywords

8 BROMO CYCLIC GMP; ADENOSINE DIPHOSPHATE; ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; GLUCOSE; GLYCERYL TRINITRATE; NITRIC OXIDE; SODIUM NITRATE; SODIUM NITRITE;

EID: 0032905354     PISSN: 08675910     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (10)

References (62)
  • 1
    • 0019195506 scopus 로고
    • The obligatory role of endothelial cells in the relaxation of arterial smooth muscle by acetylcholine
    • Furchgott MH, Zawadzki JV. The obligatory role of endothelial cells in the relaxation of arterial smooth muscle by acetylcholine. Nature 1980; 288: 373-376
    • (1980) Nature , vol.288 , pp. 373-376
    • Furchgott, M.H.1    Zawadzki, J.V.2
  • 2
    • 0006385341 scopus 로고
    • A new bioregulatory system: Nitric oxide from L-arginine
    • Kostić MM. A new bioregulatory system: Nitric oxide from L-arginine. Iugosl. Physiol Pharmacol Acta 1993; 29: 3-34.
    • (1993) Iugosl. Physiol Pharmacol Acta , vol.29 , pp. 3-34
    • Kostić, M.M.1
  • 3
    • 0029437225 scopus 로고
    • Reactions between nitric oxide, superoxide and peroxynitrite: Footprints of peroxynitrite in vivo
    • Ignarro L, Murad F (eds) San Diego, Academic Press
    • Crow JP, Beckman JS. Reactions between nitric oxide, superoxide and peroxynitrite: Footprints of peroxynitrite in vivo. In: Nitric Oxide: Biochemistry, Molecular Biology and Therapeutic Implications. Ignarro L, Murad F (eds) San Diego, Academic Press, 1995; 34, pp. 17-43.
    • (1995) Nitric Oxide: Biochemistry, Molecular Biology and Therapeutic Implications , vol.34 , pp. 17-43
    • Crow, J.P.1    Beckman, J.S.2
  • 5
    • 0020460870 scopus 로고
    • Sites of inhibition of mitochondrial electron transport in macrophage-injured neoplastic cells
    • Granger DL, Lehinger AL. Sites of inhibition of mitochondrial electron transport in macrophage-injured neoplastic cells. J Cell Biol 1982; 95: 527-535.
    • (1982) J Cell Biol , vol.95 , pp. 527-535
    • Granger, D.L.1    Lehinger, A.L.2
  • 6
    • 0022461970 scopus 로고
    • Murine cytotoxic activated macrophages inhibit aconitase in tumor cells
    • Drapier JC, Hibbs JB Jr. Murine cytotoxic activated macrophages inhibit aconitase in tumor cells. J Clin Invest 1986; 78: 790-797.
    • (1986) J Clin Invest , vol.78 , pp. 790-797
    • Drapier, J.C.1    Hibbs Jr., J.B.2
  • 7
    • 0023940538 scopus 로고
    • Differentiation of murine macrophages to express nonspecific cytotoxicity for tumor results in L-arginine-dependent inhibition of mitochondrial iron-sulfur enzymes in the macrophage effector cells
    • Drapier JC, Hibbs JB Jr. Differentiation of murine macrophages to express nonspecific cytotoxicity for tumor results in L-arginine-dependent inhibition of mitochondrial iron-sulfur enzymes in the macrophage effector cells. J Immunol 1988; 140: 2829-2838.
    • (1988) J Immunol , vol.140 , pp. 2829-2838
    • Drapier, J.C.1    Hibbs Jr., J.B.2
  • 8
    • 0029161636 scopus 로고
    • Nitric oxide regulates mitochondrial respiration and cell functions by inhibiting cytochrome oxidase
    • Brown GC. Nitric oxide regulates mitochondrial respiration and cell functions by inhibiting cytochrome oxidase. FEBS Lett 1995; 369: 136-139.
    • (1995) FEBS Lett , vol.369 , pp. 136-139
    • Brown, G.C.1
  • 9
    • 0030821015 scopus 로고    scopus 로고
    • Nitric oxide inhibition of cytochrome oxidase and mitochondrial respiration: Implications for inflammatory, neurodegenerative and ischaemic pathologies
    • Brown GC. Nitric oxide inhibition of cytochrome oxidase and mitochondrial respiration: implications for inflammatory, neurodegenerative and ischaemic pathologies. Mol Cell Biochem 1997; 174(1-2): 189-192.
    • (1997) Mol Cell Biochem , vol.174 , Issue.1-2 , pp. 189-192
    • Brown, G.C.1
  • 10
    • 0032502730 scopus 로고    scopus 로고
    • A common mechanism for the interaction of nitric oxide with the oxidized binuclear center and oxygen intermediates of cytochrome c oxidase
    • Torres J, Cooper CE, Wilson MT. A common mechanism for the interaction of nitric oxide with the oxidized binuclear center and oxygen intermediates of cytochrome c oxidase. J Biol Chem 1998; 273(15): 8756-8766.
    • (1998) J Biol Chem , vol.273 , Issue.15 , pp. 8756-8766
    • Torres, J.1    Cooper, C.E.2    Wilson, M.T.3
  • 11
    • 0031888711 scopus 로고    scopus 로고
    • Role of nitric oxide in skeletal muscle: Synthesis, distribution and functional importance
    • Reid MB. Role of nitric oxide in skeletal muscle: synthesis, distribution and functional importance. Acta Physiol Scand 1998; 162(3): 401-409.
    • (1998) Acta Physiol Scand , vol.162 , Issue.3 , pp. 401-409
    • Reid, M.B.1
  • 12
    • 0031972780 scopus 로고    scopus 로고
    • Pretreatment of astrocytes with interferon-alpha/beta prevents neuronal mitochondrial respiratory chain damage
    • Stewart VC, Land JM, Clark JB, Heales SJ. Pretreatment of astrocytes with interferon-alpha/beta prevents neuronal mitochondrial respiratory chain damage. J Neurochem 1998; 70(1): 432-434.
    • (1998) J Neurochem , vol.70 , Issue.1 , pp. 432-434
    • Stewart, V.C.1    Land, J.M.2    Clark, J.B.3    Heales, S.J.4
  • 13
    • 0027945838 scopus 로고
    • Nitric oxide potently and reversibly deenergizes mitochondria at low oxygen tension
    • Schweizer M, Richter C. Nitric oxide potently and reversibly deenergizes mitochondria at low oxygen tension. Biochem Biophys Res Commun 1994; 204(1): 169-175.
    • (1994) Biochem Biophys Res Commun , vol.204 , Issue.1 , pp. 169-175
    • Schweizer, M.1    Richter, C.2
  • 14
    • 0031281447 scopus 로고    scopus 로고
    • Nitric oxide induced contractile dysfunction is related to a reduction myocardial energy generation
    • Keim M, Schafer S, Dahmann R et al. Nitric oxide induced contractile dysfunction is related to a reduction myocardial energy generation. Cardiovasc Res 1997; 36(2): 185-194.
    • (1997) Cardiovasc Res , vol.36 , Issue.2 , pp. 185-194
    • Keim, M.1    Schafer, S.2    Dahmann, R.3
  • 15
    • 0026795982 scopus 로고
    • Nitric oxide causes ADP-ribosylation and inhibition of glyceraldehyde-3-phosphate dehydrogenase
    • Dimmeler S, Lottspeich F, Brüne B. Nitric oxide causes ADP-ribosylation and inhibition of glyceraldehyde-3-phosphate dehydrogenase. J Biol Chem 1992; 267(24): 16771-16774.
    • (1992) J Biol Chem , vol.267 , Issue.24 , pp. 16771-16774
    • Dimmeler, S.1    Lottspeich, F.2    Brüne, B.3
  • 17
    • 0030028219 scopus 로고    scopus 로고
    • Posttranslational modification of glyceraldehyde-3-phosphate dehydrogenasc by S-nitrosylation and subsequent NADH attachment
    • Mohr S, Stamler JS, Brune B. Posttranslational modification of glyceraldehyde-3-phosphate dehydrogenasc by S-nitrosylation and subsequent NADH attachment. J Biol Chem 1996; 271(8): 4209-4214.
    • (1996) J Biol Chem , vol.271 , Issue.8 , pp. 4209-4214
    • Mohr, S.1    Stamler, J.S.2    Brune, B.3
  • 18
    • 0006389233 scopus 로고    scopus 로고
    • Nitric oxide induces a transmembrane signal in human erythrocytes involving glyceradehyde 3-phosphate dehydrogenase and Band 3
    • Moncada S, Stamler J, Gross S, Higgs EA (eds) London Portland Press Ltd
    • Mallozzi C, Di Stasi AMM, Minetti M. Nitric oxide induces a transmembrane signal in human erythrocytes involving glyceradehyde 3-phosphate dehydrogenase and Band 3. In: The Biology of Initric Oxide 5. Moncada S, Stamler J, Gross S, Higgs EA (eds) London Portland Press Ltd, 1996, pp. 122.
    • (1996) The Biology of Initric Oxide 5 , pp. 122
    • Mallozzi, C.1    Di Stasi, A.M.M.2    Minetti, M.3
  • 19
    • 0030722362 scopus 로고    scopus 로고
    • Peroxynitrite modulates tyrosine-dependent signal transduction pathway of human erythrocyte band 3
    • Mallozzi C, Di Stasi AM, Minetti M. Peroxynitrite modulates tyrosine-dependent signal transduction pathway of human erythrocyte band 3. FASEB J 1997; 11(14); 1281-1290.
    • (1997) FASEB J , vol.11 , Issue.14 , pp. 1281-1290
    • Mallozzi, C.1    Di Stasi, A.M.2    Minetti, M.3
  • 20
    • 0023277458 scopus 로고
    • Correlation between nitric oxide formation during degradation of organic nitrates and activation of guanylate cyclase
    • Feelisch M, Noack E. Correlation between nitric oxide formation during degradation of organic nitrates and activation of guanylate cyclase. Eur J Pharmacol 1987; 139: 19-30.
    • (1987) Eur J Pharmacol , vol.139 , pp. 19-30
    • Feelisch, M.1    Noack, E.2
  • 21
    • 0026695136 scopus 로고
    • Dependence of the metabolism of nitric oxide (NO) in healthy human blood on the oxygenation of its red cell haemoglobin
    • Wennmalm A, Benthin G, Petersson AS. Dependence of the metabolism of nitric oxide (NO) in healthy human blood on the oxygenation of its red cell haemoglobin. Br J Pharmacol 1992; 106: 507-508.
    • (1992) Br J Pharmacol , vol.106 , pp. 507-508
    • Wennmalm, A.1    Benthin, G.2    Petersson, A.S.3
  • 23
    • 0006351561 scopus 로고    scopus 로고
    • Mechanism of action of nitrovasodilators - The nitric oxide-cyclic GMP signal transduction pathway
    • Münzel Th, Harrison DG, Just H (eds). Borken Medizin & Wissenschaft Verlag
    • Ignarro LJ. Mechanism of action of nitrovasodilators - the nitric oxide-cyclic GMP signal transduction pathway. In: Nitrates in Cardiovascular Disease. Basic Mechanism of Action, Tolerance Phenomena, Clinical Applications. Münzel Th, Harrison DG, Just H (eds). Borken Medizin & Wissenschaft Verlag, 1996, pp. 21-23.
    • (1996) Nitrates in Cardiovascular Disease. Basic Mechanism of Action, Tolerance Phenomena, Clinical Applications , pp. 21-23
    • Ignarro, L.J.1
  • 26
  • 27
    • 0020328093 scopus 로고
    • Quantification of pathways of glucose utilization and balance of energy metabolism of rabbit reticulocytes
    • Siems W, Müller M, Dumdey R, Holzhütter H-G, Rathmann J, Rapoport SM. Quantification of pathways of glucose utilization and balance of energy metabolism of rabbit reticulocytes. Eur J Biochem 1982; 124: 567-576.
    • (1982) Eur J Biochem , vol.124 , pp. 567-576
    • Siems, W.1    Müller, M.2    Dumdey, R.3    Holzhütter, H.-G.4    Rathmann, J.5    Rapoport, S.M.6
  • 28
    • 0000002475 scopus 로고
    • Determination of glucose with hexokinase and glucose-6-phosphate dehydrogenase
    • Bergmeyer HU (ed). New York, Academic Press
    • Bergmeyer HU, Bernt E, Schmidt F, Stork H. Determination of glucose with hexokinase and glucose-6-phosphate dehydrogenase. In: Methods of Enzymatic Analysis. Bergmeyer HU (ed). New York, Academic Press, 1974, pp. 1196-1201.
    • (1974) Methods of Enzymatic Analysis , pp. 1196-1201
    • Bergmeyer, H.U.1    Bernt, E.2    Schmidt, F.3    Stork, H.4
  • 29
    • 0000831018 scopus 로고
    • L-(+)-lactate. Determination with lactate dehydrogenase and NAD
    • Bergmeyer HU (ed.) New York, Academic Press
    • Gutmann I, Wahlefeld AN.L-(+)-lactate. Determination with lactate dehydrogenase and NAD. In: Methods of Enzymatic Analysis. Bergmeyer HU (ed.) New York, Academic Press, 1974, pp. 1464-1468.
    • (1974) Methods of Enzymatic Analysis , pp. 1464-1468
    • Gutmann, I.1    Wahlefeld, A.N.2
  • 30
    • 0043135692 scopus 로고
    • D-glycerate-2,3-diphosphate
    • Bergmeyer HU (ed). New York, Academic Press
    • Michal G. D-glycerate-2,3-diphosphate. In: Methods of Enzymatic Analysis. Bergmeyer HU (ed). New York, Academic Press, 1974, pp. 1433-1438.
    • (1974) Methods of Enzymatic Analysis , pp. 1433-1438
    • Michal, G.1
  • 31
    • 0001262581 scopus 로고
    • Pyruvate, phosphoenolpyruvate and d-glycerate-2-phosphate
    • Bergmeyer HU (ed). New York Academic Press
    • Czok R, Lamprecht W. Pyruvate, phosphoenolpyruvate and d-glycerate-2-phosphate. In: Methods of Enzymatic Analysis. Bergmeyer HU (ed). New York Academic Press, 1974, pp. 1446-1451.
    • (1974) Methods of Enzymatic Analysis , pp. 1446-1451
    • Czok, R.1    Lamprecht, W.2
  • 32
    • 0000777914 scopus 로고
    • Adenosine-5′-monophosphate
    • Bergmeyer HU (ed). New York, Academic Press
    • Jaworek D, Gruber W, Bergmeyer. HU. Adenosine-5′-monophosphate. In: Methods of Enzymatic. Analysis. Bergmeyer HU (ed). New York, Academic Press, 1974, pp. 2127-2131.
    • (1974) Methods of Enzymatic. Analysis , pp. 2127-2131
    • Jaworek, D.1    Gruber, W.2    Bergmeyer, H.U.3
  • 33
    • 0002633963 scopus 로고
    • Adenosine-5′-triphosphate
    • Bergmeyer HU (ed). New York, Academic Press
    • Lamprecht W, Trautschold I. Adenosine-5′-triphosphate. In: Methods of Enzymatic Analysis. Bergmeyer HU (ed). New York, Academic Press, 1974, pp. 2101-2110.
    • (1974) Methods of Enzymatic Analysis , pp. 2101-2110
    • Lamprecht, W.1    Trautschold, I.2
  • 34
    • 4143150387 scopus 로고
    • Hypoxanthine
    • Bergmeyer HU (ed). New York, Academic Press
    • Jorgensen S: Hypoxanthine. In: Methods of Enzymatic Analysis. Bergmeyer HU (ed). New York, Academic Press, 1974, pp. 1941-1945.
    • (1974) Methods of Enzymatic Analysis , pp. 1941-1945
    • Jorgensen, S.1
  • 36
    • 0002477126 scopus 로고
    • Quantitative evaluation and statistical analysis of drug action
    • Oxford, Blackwell Scientific
    • Bowman WC, Rand MJ. Quantitative evaluation and statistical analysis of drug action. In: Textbook of Pharmacology. Oxford, Blackwell Scientific, 1980, 41.1.-41.48.
    • (1980) Textbook of Pharmacology
    • Bowman, W.C.1    Rand, M.J.2
  • 37
    • 0024991324 scopus 로고
    • Catabolism of adenine nucleotides in rabbit red blood cells
    • Rapoport I, Drung I, Rapoport SM. Catabolism of adenine nucleotides in rabbit red blood cells. Biomed Biochim Acta 1990; 49(1): 11-16.
    • (1990) Biomed Biochim Acta , vol.49 , Issue.1 , pp. 11-16
    • Rapoport, I.1    Drung, I.2    Rapoport, S.M.3
  • 39
    • 0029791638 scopus 로고    scopus 로고
    • Uncoupling of mitochondrial oxidative phosphorylation alters lipid peroxidation-derived free radical production but not recovery of postischemic rat hearts and post-hypoxic endothelial cells
    • Blasig IE, Dickens BF, Weglicki WB, Kramer JH. Uncoupling of mitochondrial oxidative phosphorylation alters lipid peroxidation-derived free radical production but not recovery of postischemic rat hearts and post-hypoxic endothelial cells. Mol Cell Biochem 1996; 160-161: 167-177.
    • (1996) Mol Cell Biochem , vol.160-161 , pp. 167-177
    • Blasig, I.E.1    Dickens, B.F.2    Weglicki, W.B.3    Kramer, J.H.4
  • 40
    • 17344371804 scopus 로고    scopus 로고
    • Mitochondrial manganese superoxide dismutase prevents neural apoptosis and reduces ischemic brain injury: Suppression of peroxynitrite production, lipid peroxidation, and mitochondrial dysfunction
    • Keller JN, Kindy MS, Holtsberg FW et al. Mitochondrial manganese superoxide dismutase prevents neural apoptosis and reduces ischemic brain injury: suppression of peroxynitrite production, lipid peroxidation, and mitochondrial dysfunction. J Neurosci 1998; 18(2): 687-697.
    • (1998) J Neurosci , vol.18 , Issue.2 , pp. 687-697
    • Keller, J.N.1    Kindy, M.S.2    Holtsberg, F.W.3
  • 41
    • 6544281348 scopus 로고    scopus 로고
    • Nitric oxide promotes oxygen free radicals release in heart mitochondria and submitochondrial particles
    • Moncada S, Stamler J, Gross S, Higgs EA (eds). London, Portland Press Ltd
    • Poderoso JJ, Carreras MC, Lisdero C, Schopfer F, Riobo N, Boveris A. Nitric oxide promotes oxygen free radicals release in heart mitochondria and submitochondrial particles. In: The Biology of Nitric Oxide 5. Moncada S, Stamler J, Gross S, Higgs EA (eds). London, Portland Press Ltd, 1996, pp. 121.
    • (1996) The Biology of Nitric Oxide 5 , pp. 121
    • Poderoso, J.J.1    Carreras, M.C.2    Lisdero, C.3    Schopfer, F.4    Riobo, N.5    Boveris, A.6
  • 42
    • 0032079478 scopus 로고    scopus 로고
    • Production of nitric oxide by mitochondria
    • Giulivi C, Poderoso JJ, Boveris A. Production of nitric oxide by mitochondria. J Biol Chem 1998; 273(18): 11038-11043.
    • (1998) J Biol Chem , vol.273 , Issue.18 , pp. 11038-11043
    • Giulivi, C.1    Poderoso, J.J.2    Boveris, A.3
  • 43
    • 0023664797 scopus 로고
    • Fo portion of Echerichia coli ATP synthase: Orientation of subunit c in the membrane
    • Deckers-Hebestreit G, Schmid R, Kiltz H, Altendorf K. Fo portion of Echerichia coli ATP synthase: Orientation of subunit c in the membrane. Biochemistry 1987; 26: 5486-5492.
    • (1987) Biochemistry , vol.26 , pp. 5486-5492
    • Deckers-Hebestreit, G.1    Schmid, R.2    Kiltz, H.3    Altendorf, K.4
  • 47
    • 0029875840 scopus 로고    scopus 로고
    • S-nitrosohaemoglobin a dynamic activity of blood involved in vascular control
    • Jia L, Bonaventura C, Bonaventura J, Stamler JS. S-nitrosohaemoglobin A dynamic activity of blood involved in vascular control. Nature 1996; 380: 221-226.
    • (1996) Nature , vol.380 , pp. 221-226
    • Jia, L.1    Bonaventura, C.2    Bonaventura, J.3    Stamler, J.S.4
  • 48
    • 0032570313 scopus 로고    scopus 로고
    • Cell-free and erythrocytic S-nitrosohemoglobin inhibits human platelet aggregation
    • Pawloski JR, Swaminathan RV, Stamler JS. Cell-free and erythrocytic S-nitrosohemoglobin inhibits human platelet aggregation. Circulation 1998; 97(3): 263-267.
    • (1998) Circulation , vol.97 , Issue.3 , pp. 263-267
    • Pawloski, J.R.1    Swaminathan, R.V.2    Stamler, J.S.3
  • 49
    • 0032495529 scopus 로고    scopus 로고
    • Reactions between nitric oxide and haemoglobin under physiological conditions
    • Gow AJ, Stamler JS. Reactions between nitric oxide and haemoglobin under physiological conditions. Nature 1998; 391(6663): 169-173.
    • (1998) Nature , vol.391 , Issue.6663 , pp. 169-173
    • Gow, A.J.1    Stamler, J.S.2
  • 50
    • 0024352104 scopus 로고
    • Heme-dependent activation of soluble guanylate cyclase by nitric oxide: Regulation of enzyme activity by porphyrins and methalloporphyrins
    • Ignarro LJ. Heme-dependent activation of soluble guanylate cyclase by nitric oxide: Regulation of enzyme activity by porphyrins and methalloporphyrins. Semin Hematol 1989; 26: 63-76.
    • (1989) Semin Hematol , vol.26 , pp. 63-76
    • Ignarro, L.J.1
  • 51
    • 0026551016 scopus 로고
    • Haem-dependent activation of cytosolic guanylate cyclase by nitric oxide: A widespread signal transduction mechanism
    • Ignarro LJ. Haem-dependent activation of cytosolic guanylate cyclase by nitric oxide: A widespread signal transduction mechanism. Biochem Soc Trans 1992; 20(2): 465-469.
    • (1992) Biochem Soc Trans , vol.20 , Issue.2 , pp. 465-469
    • Ignarro, L.J.1
  • 52
    • 0028320894 scopus 로고
    • Regulation of cytosolic guanylyl cyclase by nitric oxide: The NO-cyclic GMP signal transduction system
    • Murad F. Regulation of cytosolic guanylyl cyclase by nitric oxide: The NO-cyclic GMP signal transduction system. Adv Pharmacol 1994; 26: 19-33.
    • (1994) Adv Pharmacol , vol.26 , pp. 19-33
    • Murad, F.1
  • 53
    • 0029816509 scopus 로고    scopus 로고
    • Role of endothelium-derived nitric oxide in the modulation of canine myocardial mitochondrial respiration in vitro
    • Xie YW, Shen W, Zhao G, Xu X, Wolin MS, Hintze TH. Role of endothelium-derived nitric oxide in the modulation of canine myocardial mitochondrial respiration in vitro. Circ Res 1996; 79: 381-387.
    • (1996) Circ Res , vol.79 , pp. 381-387
    • Xie, Y.W.1    Shen, W.2    Zhao, G.3    Xu, X.4    Wolin, M.S.5    Hintze, T.H.6
  • 54
    • 0025817680 scopus 로고
    • The biochemical pathways of nitric oxide formation from nitrovasodilators: Appropriate choice of exogenous NO donors and aspects of preparation and handling of aqueous NO solutions
    • Feelisch M. The biochemical pathways of nitric oxide formation from nitrovasodilators: Appropriate choice of exogenous NO donors and aspects of preparation and handling of aqueous NO solutions. J Cardiovasc Pharmacol 1991; 17 (Suppl. 3): 25-33.
    • (1991) J Cardiovasc Pharmacol , vol.17 , Issue.3 SUPPL. , pp. 25-33
    • Feelisch, M.1
  • 55
    • 0028070186 scopus 로고
    • Kinetics of the reaction of nitric oxide with oxygen in aqueous solutions
    • Lewis RS, Deen WM. Kinetics of the reaction of nitric oxide with oxygen in aqueous solutions. Chem Res Toxicol 1994; 7: 568-574.
    • (1994) Chem Res Toxicol , vol.7 , pp. 568-574
    • Lewis, R.S.1    Deen, W.M.2
  • 56
    • 0029445068 scopus 로고
    • Chemistry of nitric oxide: Biologically relevant aspects
    • Ignarro L, Murad F (eds). San Diego, Academic Press
    • Fukuto JM. Chemistry of nitric oxide: Biologically relevant aspects. In: Nitric Oxide: Biochemistry, Molecular Biology and Therapeutic Implications. Ignarro L, Murad F (eds). San Diego, Academic Press, 1995, 34, pp. 1-15.
    • (1995) Nitric Oxide: Biochemistry, Molecular Biology and Therapeutic Implications , vol.34 , pp. 1-15
    • Fukuto, J.M.1
  • 57
    • 0027015063 scopus 로고
    • Purification of erythrocyte cytochrome P-450 from goat and chick
    • Patil SS, Makhija SJ, Pawar SS. Purification of erythrocyte cytochrome P-450 from goat and chick. Indian J Biochem Biophys 1992; 29(6): 516-518.
    • (1992) Indian J Biochem Biophys , vol.29 , Issue.6 , pp. 516-518
    • Patil, S.S.1    Makhija, S.J.2    Pawar, S.S.3
  • 58
    • 0029928663 scopus 로고    scopus 로고
    • Influence of erythrocyte glutathione S-transferase T1 on sister chromatid exchanges induced by diepoxybutane in cultured human lymphocytes
    • Pelin K, Hirvonen A, Norppa H. Influence of erythrocyte glutathione S-transferase T1 on sister chromatid exchanges induced by diepoxybutane in cultured human lymphocytes. Mutagenesis 1996; 11(2): 213-215.
    • (1996) Mutagenesis , vol.11 , Issue.2 , pp. 213-215
    • Pelin, K.1    Hirvonen, A.2    Norppa, H.3
  • 59
    • 0029992218 scopus 로고    scopus 로고
    • Purification and characterization of a new glutathione S-transferases, class theta, from human erythrocytes
    • Schroder KR, Hallier E, Meyer DJ, Wiebel FA, Muller AM, Bolt HM. Purification and characterization of a new glutathione S-transferases, class theta, from human erythrocytes. Arch Toxicol 1996; 70(9) 559-566.
    • (1996) Arch Toxicol , vol.70 , Issue.9 , pp. 559-566
    • Schroder, K.R.1    Hallier, E.2    Meyer, D.J.3    Wiebel, F.A.4    Muller, A.M.5    Bolt, H.M.6
  • 60
    • 0031021755 scopus 로고    scopus 로고
    • Erythrocyte glutathione-S-transferase activity in animal species
    • Vodela JK, Dalvi RR. Erythrocyte glutathione-S-transferase activity in animal species. Vet Hum Toxicol 1997; 39(1): 9-11.
    • (1997) Vet Hum Toxicol , vol.39 , Issue.1 , pp. 9-11
    • Vodela, J.K.1    Dalvi, R.R.2
  • 61
    • 0025357203 scopus 로고
    • Purification and characterization of glutathione transferases with an activity toward nitroglycerin from human aorta and heart
    • Tsuchida S, Maki T, Sato K. Purification and characterization of glutathione transferases with an activity toward nitroglycerin from human aorta and heart. J Biol Chem 1990; 265: 7150-7157.
    • (1990) J Biol Chem , vol.265 , pp. 7150-7157
    • Tsuchida, S.1    Maki, T.2    Sato, K.3
  • 62
    • 0026680866 scopus 로고
    • Cytochrome P-450 mediates bioactivation of organic nitrates
    • Schröder H. Cytochrome P-450 mediates bioactivation of organic nitrates. J Pharmacol Exp Ther 1992; 262(1): 298-302.
    • (1992) J Pharmacol Exp Ther , vol.262 , Issue.1 , pp. 298-302
    • Schröder, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.